HOMCOS(prot_sch_conbars.cgi):

		Contact Molecules for Homologous Proteins
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PID	QueryLength	Homolgous Sequence in PDB	UniProt Query	TITLE
3960037	165	500	P62937(PPIA_HUMAN)	RecName: Full=Peptidyl-prolyl cis-trans isomerase A; Short=PPIase A; EC=5.2.1.8 ;AltName: Full=Cyclophilin A;AltName: Full=Cyclosporin A-binding protein;AltName: Full=Rotamase A;Contains: RecName: Full=Peptidyl-prolyl cis-trans isomerase A, N-terminally processed;
QUERYSEQ	MVNPTVFFDIAVDGEPLGRVSFELFADKVPKTAENFRALSTGEKGFGYKGSCFHRIIPGFMCQGGDFTRHNGTGGKSIYGEKFEDENFILKHTGPGILSMANAGPNTNGSQFFICTAKTEWLDGKHVVFGKVKEGMNIVEAMERFGSRNG KTSKKITIADCGQLE

[BLAST file for PDB] (plain) (bar) (multiple alignment) [BLAST for UniProt: (plain) (bar) (multiple alignment) (PSSM file) ]

UniProt Feature Tables [P62937(PPIA_HUMAN)]

165
	region	name	description
	1-165	CHAIN	/note="Peptidyl-prolyl cis-trans isomerase A" /id="PRO_0000423240"
	2-165	CHAIN	/note="Peptidyl-prolyl cis-trans isomerase A, N-terminally processed" /id="PRO_0000064115"
	7-163	DOMAIN	/note="PPIase cyclophilin-type"
	1-1	DISORDER	predicted by DISOPRED

MONOMER

165

pdb_id a¹ identity[%]² description

8g9p D 100.0 PPIA_HUMAN Peptidyl-prolyl cis-trans isomerase A

1.a¹:asym_id for the homologue. 2.identity[%]²:sequence identity between the query and the homologue.

HETERO

165 pdb_id contact mol homologue

a³ description a⁴ identity[%]⁵ Ncon⁶ description

1awq[14] B PEPTIDE FROM THE HIV-1 CAPSID PROTEIN[6 aa] A 100.0
/100.0 15
/15 PPIA_HUMAN CYCLOPHILIN A

1awu[7] B PEPTIDE FROM THE HIV-1 CAPSID PROTEIN[6 aa] A 100.0
/100.0 12
/12 PPIA_HUMAN CYCLOPHILIN A

1bck[1] B CYCLOSPORIN C[11 aa] A 100.0
/100.0 15
/15 PPIA_HUMAN PEPTIDYL-PROLYL CIS-TRANS ISOMERASE A

1cwf[4] B CYCLOSPORIN D[11 aa] A 100.0
/100.0 14
/14 PPIA_HUMAN PEPTIDYL-PROLYL CIS-TRANS ISOMERASE A

1cwo[1] B CYCLOSPORIN C[11 aa] A 100.0
/100.0 11
/11 PPIA_HUMAN PEPTIDYL-PROLYL CIS-TRANS ISOMERASE A

1fgl[1] B GAG_HV1W2 HIV-1 GAG PROTEIN[12 aa] A 100.0
/100.0 14
/14 PPIA_HUMAN CYCLOPHILIN A

1m63[3] A P2BA_HUMAN SERINE/THREONINE PROTEIN PHOSPHATASE 2B CATALYTIC .. C 100.0
/100.0 6
/6 PPIA_HUMAN PEPTIDYL-PROLYL CIS-TRANS ISOMERASE A

1m63[2] E P2BA_HUMAN SERINE/THREONINE PROTEIN PHOSPHATASE 2B CATALYTIC .. C 100.0
/100.0 4
/4 PPIA_HUMAN PEPTIDYL-PROLYL CIS-TRANS ISOMERASE A

1m63[3] B CANB1_HUMAN CALCINEURIN B SUBUNIT ISOFORM 1[158 aa] C 100.0
/100.0 5
/5 PPIA_HUMAN PEPTIDYL-PROLYL CIS-TRANS ISOMERASE A

1m63[2] F CANB1_HUMAN CALCINEURIN B SUBUNIT ISOFORM 1[160 aa] C 100.0
/100.0 1
/1 PPIA_HUMAN PEPTIDYL-PROLYL CIS-TRANS ISOMERASE A

1rmh[2] C AAPF PEPTIDE SUBSTRATE[6 aa] A 100.0
/100.0 14
/14 CYPH_HUMAN CYCLOPHILIN A

1rmh[2] D AAPF PEPTIDE SUBSTRATE[6 aa] A 100.0
/100.0 1
/1 CYPH_HUMAN CYCLOPHILIN A

1vbs[3] B TETRAPEPTIDE[5 aa] A 100.0
/100.0 13
/13 CYPH_HUMAN CYCLOPHILIN A

1zkf[2] C Suc-ALA-GLY-PRO-PHE-pNA[6 aa] A 100.0
/100.0 13
/13 PPIA_HUMAN Peptidyl-prolyl cis-trans isomerase A

2ms4[1] B Peptide[9 aa] A 100.0
/100.0 17
/17 PPIA_HUMAN Peptidyl-prolyl cis-trans isomerase A

2xgy[1] A RELIK CAPSID N-TERMINAL DOMAIN[129 aa] B 100.0
/100.0 18
/18 PPIA_HUMAN PEPTIDYL-PROLYL CIS-TRANS ISOMERASE A

5fjb[13] A GAG_HV1B1 GAG POLYPROTEIN[218 aa] C 100.0
/100.0 15
/15 PPIA_HUMAN PEPTIDYL-PROLYL CIS-TRANS ISOMERASE A

5fjb[3] B GAG_HV1B1 GAG POLYPROTEIN[218 aa] C 100.0
/100.0 2
/2 PPIA_HUMAN PEPTIDYL-PROLYL CIS-TRANS ISOMERASE A

6y9v[6] M POL_HV1LW Gag-Pol polyprotein[220 aa] G 100.0
/100.0 7
/7 PPIA_HUMAN Peptidyl-prolyl cis-trans isomerase A

6i42[1] B SYUA_HUMAN Alpha-synuclein[13 aa] A 100.0
/100.0 17
/17 PPIA_HUMAN Peptidyl-prolyl cis-trans isomerase A

7abt[1] B PRO-ARG-PRO-ARG-PRO-ARG-PRO-ARG[8 aa] A 100.0
/100.0 11
/11 PPIA_HUMAN Peptidyl-prolyl cis-trans isomerase A

7upn[2] B VIF_VILVK Virion infectivity factor[208 aa] A 100.0
/100.0 21
/21 PPIA_HUMAN Peptidyl-prolyl cis-trans isomerase A

7uxj[4] E FP29102[12 aa] A 100.0
/100.0 13
/13 PPIA_HUMAN Peptidyl-prolyl cis-trans isomerase A

7uxm[3] D FP29092[18 aa] A 100.0
/100.0 18
/18 PPIA_HUMAN Peptidyl-prolyl cis-trans isomerase A

7uxn[1] B FP29103[12 aa] A 100.0
/100.0 16
/16 PPIA_HUMAN Peptidyl-prolyl cis-trans isomerase A

8g9p[25] B RASK_HUMAN GTPase KRas[170 aa] C 100.0
/100.0 9
/9 PPIA_HUMAN Peptidyl-prolyl cis-trans isomerase A

8hz8[1] B NRF2 peptide[4 aa] A 100.0
/100.0 11
/11 PPIA_HUMAN Peptidyl-prolyl cis-trans isomerase A, N-terminall..

8tbi[2] B RASN_HUMAN GTPase NRas[170 aa] C 100.0
/100.0 10
/10 PPIA_HUMAN Peptidyl-prolyl cis-trans isomerase A

7pcj[2] F Aromatic foldamer[7 aa] A 50.0
/99.4 2
/2 PPIA_HUMAN Peptidyl-prolyl cis-trans isomerase A

4dgb[1] B GAG_HV2RO capsid protein[6 aa] A 100.0
/98.8 8
/8 B0LJC8_MACMU TRIMCyp

5hsv[4] E Alisporivir[11 aa] A 100.0
/100.0 14
/14 PPIA_CHLAE Peptidyl-prolyl cis-trans isomerase A

6hmz[1] B Cyclosporin[11 aa] A 92.3
/74.1 13
/13 A0A078GRH6_BRANA Peptidyl-prolyl cis-trans isomerase

5z56[2] CA SF3B2_HUMAN Splicing factor 3B subunit 2[183 aa] GB 100.0
/67.8 2
/2 PPIE_HUMAN Peptidyl-prolyl cis-trans isomerase E

8ch6[1] L SF3B2_HUMAN Splicing factor 3B subunit 2[198 aa] DB 83.3
/67.8 6
/6 PPIE_HUMAN Peptidyl-prolyl cis-trans isomerase E

5yzg[1] QA RU2A_HUMAN U2 small nuclear ribonucleoprotein A' [162 aa] ZA 33.3
/67.7 3
/3 PPIE_HUMAN Peptidyl-prolyl cis-trans isomerase E

5mqf[1] M SYF1_HUMAN Pre-mRNA-splicing factor SYF1[706 aa] MA 100.0
/67.4 9
/9 PPIE_HUMAN Peptidyl-prolyl cis-trans isomerase E

6ff7[1] HB ISY1_HUMAN Pre-mRNA-splicing factor ISY1 homolog[56 aa] DB 75.0
/67.4 8
/8 PPIE_HUMAN Peptidyl-prolyl cis-trans isomerase E

7abi[1] CB SF3B2_HUMAN Splicing factor 3B subunit 2[183 aa] GA 100.0
/67.4 2
/2 PPIE_HUMAN Peptidyl-prolyl cis-trans isomerase E

7abi[1] E SF3B4_HUMAN Splicing factor 3B subunit 4[78 aa] GA 62.5
/67.4 8
/8 PPIE_HUMAN Peptidyl-prolyl cis-trans isomerase E

1ak4[26] D POL_HV1N5 HIV-1 CAPSID[145 aa] A 100.0
/100.0 15
/15 PPIA_HUMAN CYCLOPHILIN A

4lqw[2] D POL_HV1N5 Capsid protein p24[141 aa] A 68.8
/66.7 16
/16 RBP2_HUMAN E3 SUMO-protein ligase RanBP2

1vdn[1] B (ACE)AAPA(MCM)[6 aa] A 83.3
/66.7 12
/12 CYPH_YEAST Cyclophilin A

7wff[2] B A0A1B1W4Z4_ARATH NAD(P)H-quinone oxidoreductase subunit 2, chloropl.. Q 100.0
/66.0 1
/1 PNSL5_ARATH Isoform 2 of Photosynthetic NDH subunit of lumenal..

7wff[2] D A0A1B1W4Z0_ARATH NAD(P)H-quinone oxidoreductase chain 4, chloroplas.. Q 80.0
/66.0 5
/6 PNSL5_ARATH Isoform 2 of Photosynthetic NDH subunit of lumenal..

7wff[2] P PNSL4_ARATH Photosynthetic NDH subunit of lumenal location 4, .. Q 90.5
/66.0 21
/21 PNSL5_ARATH Isoform 2 of Photosynthetic NDH subunit of lumenal..

3ici[1] C Calnexin[9 aa] A 25.0
/65.6 4
/10 PPIB_HUMAN Peptidyl-prolyl cis-trans isomerase B

7eu3[2] D S4Z8N2_HORVS NAD(P)H-quinone oxidoreductase chain 4, chloroplas.. T 0.0
/65.0 1
/3 Photosynthetic NDH subunit of subcomplex L5

7eu3[2] S Photosynthetic NDH subunit of subcomplex L4[130 aa.. T 86.7
/65.0 15
/15 Photosynthetic NDH subunit of subcomplex L5

5yba[1] A Myb1 peptide[6 aa] B 88.2
/64.8 17
/17 A2DT06_TRIVA Peptidyl-prolyl cis-trans isomerase

5yba[1] C Myb1 peptide[5 aa] D 100.0
/64.8 13
/13 A2DT06_TRIVA Peptidyl-prolyl cis-trans isomerase

1mzw[1] B PRP4_HUMAN U4/U6 snrnp 60kDa protein[31 aa] A 53.3
/55.8 15
/15 PPIH_HUMAN U-snRNP-associated cyclophilin

5o9z[9] F PRP4_HUMAN U4/U6 small nuclear ribonucleoprotein Prp4[420 aa].. M 57.1
/55.8 7
/7 PPIH_HUMAN Peptidyl-prolyl cis-trans isomerase H

5o9z[6] Q WBP4_HUMAN WW domain-binding protein 4[75 aa] M 0.0
/55.8 5
/5 PPIH_HUMAN Peptidyl-prolyl cis-trans isomerase H

7ane[1] AD mL52[195 aa] VC 0.0
/53.8 1
/2 Q4QBK2_LEIMA Peptidyl-prolyl cis-trans isomerase

7ane[1] BD Q4QIB3_LEIMA mL49[207 aa] VC 16.7
/53.8 6
/6 Q4QBK2_LEIMA Peptidyl-prolyl cis-trans isomerase

7ane[1] ED Q4QJB6_LEIMA mL63[139 aa] VC 52.6
/53.8 19
/19 Q4QBK2_LEIMA Peptidyl-prolyl cis-trans isomerase

7ane[1] RC Q4Q547_LEIMA mL79[275 aa] VC 40.0
/53.8 5
/14 Q4QBK2_LEIMA Peptidyl-prolyl cis-trans isomerase

7ane[1] TB Q9U0Z7_LEIMA uL30m[150 aa] VC 33.3
/53.8 6
/9 Q4QBK2_LEIMA Peptidyl-prolyl cis-trans isomerase

7ane[1] YB Q4Q5A3_LEIMA mL38[468 aa] VC 42.9
/53.8 7
/13 Q4QBK2_LEIMA Peptidyl-prolyl cis-trans isomerase

1c5f[8] B CYCLOSPORIN A[11 aa] A 85.7
/50.9 14
/14 CYP1_BRUMA PEPTIDYL-PROLYL CIS-TRANS ISOMERASE 1

1cwa[81] B CYCLOSPORIN A[11 aa] A 100.0
/100.0 13
/13 CYPH_HUMAN PEPTIDYL-PROLYL CIS-TRANS ISOMERASE A

1qng[3] B CYCLOSPORIN A[11 aa] A 100.0
/63.5 13
/13 Q25756 PEPTIDYL-PROLYL CIS-TRANS ISOMERASE

2esl[6] G CYCLOSPORIN A[11 aa] A 100.0
/63.4 14
/14 PPIC_HUMAN Peptidyl-prolyl cis-trans isomerase C

2esl[6] K CYCLOSPORIN A[11 aa] A 100.0
/63.4 4
/4 PPIC_HUMAN Peptidyl-prolyl cis-trans isomerase C

2poy[3] D CYCLOSPORIN A[11 aa] A 100.0
/67.9 14
/14 A3FQA7_CRYPV PEPTIDYL-PROLYL CIS-TRANS ISOMERASE

2rma[30] D CYCLOSPORIN A[11 aa] A 100.0
/100.0 3
/3 PPIA_HUMAN PEPTIDYL-PROLYL CIS-TRANS ISOMERASE

2rma[30] L CYCLOSPORIN A[11 aa] A 100.0
/100.0 3
/3 PPIA_HUMAN PEPTIDYL-PROLYL CIS-TRANS ISOMERASE

2rmc[4] B CYCLOSPORIN A[11 aa] A 100.0
/57.3 13
/13 CYPC_MOUSE PEPTIDYL-PROLYL CIS-TRANS ISOMERASE C

2wfj[1] B CYCLOSPORIN A[11 aa] A 84.6
/56.6 13
/13 PPIG_HUMAN PEPTIDYL-PROLYL CIS-TRANS ISOMERASE G

3eov[3] C CYCLOSPORIN A[11 aa] A 100.0
/59.9 12
/12 Q9U9R3_LEIDO PEPTIDYL-PROLYL CIS-TRANS ISOMERASE

4jjm[2] D cyclosporin A[11 aa] A 100.0
/74.8 12
/12 D0ELH5_CITSI Peptidyl-prolyl cis-trans isomerase

8b58[2] C Cyclosporin A[11 aa] A 92.3
/53.1 13
/13 A0A7J6KAD1_TOXGO Peptidyl-prolyl cis-trans isomerase

3.a³:asym_id for the contact molecule. 4.a⁴:asym_id for the template homologue. 5.identity[%]⁵:sequence identity between the query and the template homologue only for the contact residues. Number after the slash / is sequence identity for all the aligned region. 6.Ncon⁶:number of aligned contact residues for the query. Number after the slash / is number of contact residues in the template homologue.

NUCLEOTIDE

165 pdb_id contact mol homologue

a³ description a⁴ identity[%]⁵ Ncon⁶ description

5mqf[1] RA Human gene for small nuclear RNA U2 (snRNA U2) MA 33.3
/67.4 6
/8 PPIE_HUMAN Peptidyl-prolyl cis-trans isomerase E

7ane[1] TD Large ribosomal RNA VC 0.0
/53.8 3
/8 Q4QBK2_LEIMA Peptidyl-prolyl cis-trans isomerase

3.a³:asym_id for the contact molecule. 4.a⁴:asym_id for the template homologue. 5.identity[%]⁵:sequence identity between the query and the template homologue only for the contact residues. Number after the slash / is sequence identity for all the aligned region. 6.Ncon⁶:number of aligned contact residues for the query. Number after the slash / is number of contact residues in the template homologue.

COMPOUND

165 pdb_id contact mol homologue

a³ description a⁴ identity[%]⁵ Ncon⁶ description

1e8k[3] C PRO
PROLINE[8 atoms] A 100.0
/70.3 6
/6 CYP3_CAEEL PEPTIDYL-PROLYL CIS-TRANS ISOMERASE 3

2cfe[1] C PRO
PROLINE[8 atoms] A 100.0
/71.3 5
/5 O93970_9BASI ALLERGEN

2cyh[4] C PRO
PROLINE[8 atoms] A 100.0
/100.0 5
/5 CYPH_HUMAN CYCLOPHILIN A

4n1m[1] C PRO
PROLINE[8 atoms] A 100.0
/100.0 6
/6 PPIA_HUMAN Peptidyl-prolyl cis-trans isomerase A

1nmk[2] C SFM
(13E,15E)-(3S,6S,9R,10R,11S,12S,18S,21S)-10,12-DIH.. A 100.0
/100.0 15
/15 PPIA_HUMAN Peptidyl-prolyl cis-trans isomerase A

1w8l[1] B 1P3
(3R)-1-ACETYL-3-METHYLPIPERIDINE[10 atoms] A 100.0
/100.0 7
/7 PPIA_HUMAN PEPTIDYL-PROLYL CIS-TRANS ISOMERASE A

1w8m[1] B E1P
ETHYL OXO(PIPERIDIN-1-YL)ACETATE[13 atoms] A 100.0
/100.0 7
/7 PPIA_HUMAN PEPTIDYL-PROLYL CIS-TRANS ISOMERASE A

1ynd[2] C SFA
SANGLIFEHRIN A[78 atoms] A 100.0
/100.0 18
/18 PPIA_HUMAN Peptidyl-prolyl cis-trans isomerase A

4cyh[1] B HIS
HISTIDINE[10 atoms] A 100.0
/100.0 4
/4 CYPH_HUMAN CYCLOPHILIN A

4n1n[1] B UNU
BENZAMIDE[9 atoms] A 100.0
/100.0 8
/8 PPIA_HUMAN Peptidyl-prolyl cis-trans isomerase A

4n1o[1] B LSA
1,2-BENZISOTHIAZOL-3(2H)-ONE 1,1-DIOXIDE[12 atoms].. A 100.0
/100.0 5
/5 PPIA_HUMAN Peptidyl-prolyl cis-trans isomerase A

4n1o[1] C LSA
1,2-BENZISOTHIAZOL-3(2H)-ONE 1,1-DIOXIDE[12 atoms].. A 100.0
/100.0 7
/7 PPIA_HUMAN Peptidyl-prolyl cis-trans isomerase A

4n1o[1] D LSA
1,2-BENZISOTHIAZOL-3(2H)-ONE 1,1-DIOXIDE[12 atoms].. A 100.0
/100.0 6
/6 PPIA_HUMAN Peptidyl-prolyl cis-trans isomerase A

4n1o[2] E LSA
1,2-BENZISOTHIAZOL-3(2H)-ONE 1,1-DIOXIDE[12 atoms].. A 100.0
/100.0 4
/4 PPIA_HUMAN Peptidyl-prolyl cis-trans isomerase A

4n1p[1] B WM1
pyridine-2-carboxamide[9 atoms] A 100.0
/100.0 7
/7 PPIA_HUMAN Peptidyl-prolyl cis-trans isomerase A

4n1p[1] C WM1
pyridine-2-carboxamide[9 atoms] A 100.0
/100.0 8
/8 PPIA_HUMAN Peptidyl-prolyl cis-trans isomerase A

4n1p[1] D WM1
pyridine-2-carboxamide[9 atoms] A 100.0
/100.0 2
/2 PPIA_HUMAN Peptidyl-prolyl cis-trans isomerase A

4n1q[1] B WM2
cyclohexanecarboxamide[9 atoms] A 100.0
/100.0 8
/8 PPIA_HUMAN Peptidyl-prolyl cis-trans isomerase A

4n1r[1] B WM3
benzenesulfonohydrazide[11 atoms] A 100.0
/100.0 8
/8 PPIA_HUMAN Peptidyl-prolyl cis-trans isomerase A

4n1s[2] B WM4
benzohydrazide[10 atoms] A 100.0
/100.0 6
/6 PPIA_HUMAN Peptidyl-prolyl cis-trans isomerase A

5lud[1] B 76X
pyridine-2,3-diamine[8 atoms] A 100.0
/100.0 7
/7 V9HWF5_HUMAN Peptidyl-prolyl cis-trans isomerase

5noq[1] B 93E
3-chloranylpyridin-2-amine[8 atoms] A 100.0
/100.0 7
/7 PPIA_HUMAN Peptidyl-prolyl cis-trans isomerase A

5noq[1] C 93E
3-chloranylpyridin-2-amine[8 atoms] A 100.0
/100.0 4
/4 PPIA_HUMAN Peptidyl-prolyl cis-trans isomerase A

5nor[1] B 93Q
3-methylpyridin-2-amine[8 atoms] A 100.0
/100.0 4
/4 PPIA_HUMAN Peptidyl-prolyl cis-trans isomerase A

5nor[1] C 93Q
3-methylpyridin-2-amine[8 atoms] A 100.0
/100.0 9
/9 PPIA_HUMAN Peptidyl-prolyl cis-trans isomerase A

5nos[1] B 92Z
5-azanyl-3~{H}-pyridin-6-one[8 atoms] A 100.0
/100.0 5
/5 PPIA_HUMAN Peptidyl-prolyl cis-trans isomerase A

5not[1] B 938
4-chloranylpyrimidin-5-amine[8 atoms] A 100.0
/100.0 4
/4 PPIA_HUMAN Peptidyl-prolyl cis-trans isomerase A

5not[1] C 938
4-chloranylpyrimidin-5-amine[8 atoms] A 100.0
/100.0 7
/7 PPIA_HUMAN Peptidyl-prolyl cis-trans isomerase A

5nou[1] B L60
1,3-diazinan-2-one[7 atoms] A 100.0
/100.0 6
/6 PPIA_HUMAN Peptidyl-prolyl cis-trans isomerase A

5nou[1] C L60
1,3-diazinan-2-one[7 atoms] A 100.0
/100.0 2
/2 PPIA_HUMAN Peptidyl-prolyl cis-trans isomerase A

5nou[1] D L60
1,3-diazinan-2-one[7 atoms] A 100.0
/100.0 5
/5 PPIA_HUMAN Peptidyl-prolyl cis-trans isomerase A

5nov[1] B 93B
1,3-diazinane-2-thione[7 atoms] A 100.0
/100.0 6
/6 PPIA_HUMAN Peptidyl-prolyl cis-trans isomerase A

5now[1] B L89
pyridine-3,4-diamine[8 atoms] A 100.0
/100.0 8
/8 PPIA_HUMAN Peptidyl-prolyl cis-trans isomerase A

5nox[1] B L97
2-chloranylpyridin-3-amine[8 atoms] A 100.0
/100.0 7
/7 PPIA_HUMAN Peptidyl-prolyl cis-trans isomerase A

5noy[1] B 93K
3,4-bis(azanyl)benzamide[11 atoms] A 100.0
/100.0 8
/8 PPIA_HUMAN Peptidyl-prolyl cis-trans isomerase A

5noz[1] B L99
3,4-bis(azanyl)benzohydrazide[12 atoms] A 100.0
/100.0 8
/8 PPIA_HUMAN Peptidyl-prolyl cis-trans isomerase A

5t9u[4] E 7HG
3-[(3-hydroxyphenyl)methyl]-10,12-dimethoxy-9,11-d.. A 100.0
/100.0 14
/14 PPIA_HUMAN Peptidyl-prolyl cis-trans isomerase A

5t9w[1] B 78E
3-[(3-hydroxyphenyl)methyl]-6-(propan-2-yl)-19-oxa.. A 100.0
/100.0 14
/14 PPIA_HUMAN Peptidyl-prolyl cis-trans isomerase A

5t9z[1] B 78R
11-[(3-hydroxyphenyl)methyl]-18-methoxy-17-methyl-.. A 100.0
/100.0 14
/14 PPIA_HUMAN Peptidyl-prolyl cis-trans isomerase A

5ta2[1] B 78X
11-[(3-hydroxyphenyl)methyl]-18-methoxy-2,17-dimet.. A 100.0
/100.0 14
/14 PPIA_HUMAN Peptidyl-prolyl cis-trans isomerase A

5ta4[1] B 838
18-methoxy-2,11,17-trimethyl-14-(propan-2-yl)-3-ox.. A 100.0
/100.0 14
/14 PPIA_HUMAN Peptidyl-prolyl cis-trans isomerase A

6gji[1] B F1E
ethyl 2-[[(4-aminophenyl)methyl-[(1-methyl-1,2,3-t.. A 100.0
/100.0 11
/11 PPIA_HUMAN Peptidyl-prolyl cis-trans isomerase A

6gjj[2] B L36
ethyl 2-[[(4-aminophenyl)methyl-propyl-carbamoyl]a.. A 100.0
/100.0 11
/11 PPIA_HUMAN Peptidyl-prolyl cis-trans isomerase A

6gjl[1] B F1Q
ethyl 2-[[(4-aminophenyl)methyl-(1~{H}-1,2,3,4-tet.. A 100.0
/100.0 12
/12 PPIA_HUMAN Peptidyl-prolyl cis-trans isomerase A

6gjn[1] B F0Q
1-[(4-aminophenyl)methyl]-3-[2-[(2~{R})-2-(2-bromo.. A 100.0
/100.0 15
/15 PPIA_HUMAN Peptidyl-prolyl cis-trans isomerase A

6gjp[1] B F0T
ethyl 2-[[(4-aminophenyl)methyl-(cyclopropylmethyl.. A 100.0
/100.0 11
/11 PPIA_HUMAN Peptidyl-prolyl cis-trans isomerase A

6gjr[1] B F0W
ethyl 2-[[(4-aminophenyl)methyl-[(2-methyl-1,2,3,4.. A 100.0
/100.0 13
/13 PPIA_HUMAN Peptidyl-prolyl cis-trans isomerase A

6gjy[1] B F1Z
ethyl 2-[[(4-aminophenyl)methyl-prop-2-ynyl-carbam.. A 100.0
/100.0 12
/12 PPIA_HUMAN Peptidyl-prolyl cis-trans isomerase A

6x3r[1] B ZXX
methyl (3~{S})-1-[(2~{S})-2-[[(2~{S})-2-acetamido-.. A 100.0
/100.0 12
/12 PPIA_HUMAN Peptidyl-prolyl cis-trans isomerase A

6x3y[2] B UMM
tert-butyl [(2S)-1-{[(3S,17S)-2,16-dioxo-10,15-dio.. A 100.0
/100.0 12
/12 PPIA_HUMAN Peptidyl-prolyl cis-trans isomerase A

6x4n[1] B UOD
(2R,5S,11S,14S,18E)-2,11,17,17-tetramethyl-14-(pro.. A 100.0
/100.0 12
/12 PPIA_HUMAN Peptidyl-prolyl cis-trans isomerase A

6x4o[1] B UO7
(2R,5S,11S,14S,18E)-2,11-dimethyl-14-(propan-2-yl).. A 100.0
/100.0 11
/11 PPIA_HUMAN Peptidyl-prolyl cis-trans isomerase A

6x4p[1] B UOG
(2R,5S,11S,14S,18E)-2,11,17,17-tetramethyl-14-(pro.. A 100.0
/100.0 11
/11 PPIA_HUMAN Peptidyl-prolyl cis-trans isomerase A

6x4q[1] B UOJ
(2R,5S,11S,14S,18E)-14-cyclobutyl-2,11,17,17-tetra.. A 100.0
/100.0 12
/12 PPIA_HUMAN Peptidyl-prolyl cis-trans isomerase A

7uxj[4] J WHL
N,N'-(1,4-phenylene)diacetamide[14 atoms] A 100.0
/100.0 1
/1 PPIA_HUMAN Peptidyl-prolyl cis-trans isomerase A

8g9p[2] K YV2
(2S)-2-{(5S)-7-[(2E)-4-(dimethylamino)-4-methylpen.. C 100.0
/100.0 14
/14 PPIA_HUMAN Peptidyl-prolyl cis-trans isomerase A

8tbf[18] J ZNI
(1R,5S,6r)-N-[(1P,7S,9S,13S,20M)-20-{5-(4-cyclopro.. C 100.0
/100.0 14
/14 PPIA_HUMAN Peptidyl-prolyl cis-trans isomerase A

9ax6[2] I A1AHB
(1R,2S)-N-[(1P,7S,9S,13R,20M)-21-ethyl-20-{2-[(1R).. C 100.0
/100.0 14
/14 PPIA_HUMAN Peptidyl-prolyl cis-trans isomerase A

9bg1[2] G A1AOH
(2R)-N-[(1P,7S,9S,13R,20M)-21-ethyl-20-{2-[(1S)-1-.. B 100.0
/100.0 15
/15 PPIA_HUMAN Peptidyl-prolyl cis-trans isomerase A

9bfy[2] J A1AOL
(3R)-N-[(2S)-1-{[(1M,8R,10R,14S,21M)-22-ethyl-4-hy.. C 100.0
/99.4 15
/15 PPIA_HUMAN Peptidyl-prolyl cis-trans isomerase A

8g9q[1] E YV6
methyl (3S)-1-(N-{4-[(pyridin-2-yl)disulfanyl]buta.. B 100.0
/99.4 11
/11 PPIA_HUMAN Peptidyl-prolyl cis-trans isomerase A

3rdc[1] B EA4
ethyl N-[(4-aminobenzyl)carbamoyl]glycinate[18 ato.. A 92.9
/75.5 14
/14 PPIF_HUMAN Peptidyl-prolyl cis-trans isomerase F, mitochondri..

3rdd[1] B EA4
ethyl N-[(4-aminobenzyl)carbamoyl]glycinate[18 ato.. A 100.0
/100.0 12
/12 PPIA_HUMAN Peptidyl-prolyl cis-trans isomerase A

4xnc[2] B EA4
ethyl N-[(4-aminobenzyl)carbamoyl]glycinate[18 ato.. A 92.3
/75.5 13
/13 PPIF_HUMAN Peptidyl-prolyl cis-trans isomerase F, mitochondri..

6gs6[1] B EA4
ethyl N-[(4-aminobenzyl)carbamoyl]glycinate[18 ato.. A 100.0
/99.4 11
/11 PPIA_HUMAN Peptidyl-prolyl cis-trans isomerase A

7tgu[1] B I44
(4S,7S,11R,13E,19S)-N-[2-(2-aminoethoxy)ethyl]-4-[.. A 85.0
/75.9 20
/20 PPIF_HUMAN Peptidyl-prolyl cis-trans isomerase F, mitochondri..

3r49[1] B Q8A
quinolin-8-amine[11 atoms] A 85.7
/75.5 7
/7 PPIF_HUMAN Peptidyl-prolyl cis-trans isomerase F, mitochondri..

3r49[1] C Q8A
quinolin-8-amine[11 atoms] A 25.0
/75.5 4
/4 PPIF_HUMAN Peptidyl-prolyl cis-trans isomerase F, mitochondri..

3r4g[1] B 4SO
4-sulfamoylbenzoic acid[13 atoms] A 42.9
/75.5 7
/7 PPIF_HUMAN Peptidyl-prolyl cis-trans isomerase F, mitochondri..

3r4g[1] C 4SO
4-sulfamoylbenzoic acid[13 atoms] A 60.0
/75.5 5
/5 PPIF_HUMAN Peptidyl-prolyl cis-trans isomerase F, mitochondri..

3r54[1] B FP6
pyrrolidine-1-carbaldehyde[7 atoms] A 100.0
/75.5 9
/9 PPIF_HUMAN Peptidyl-prolyl cis-trans isomerase F, mitochondri..

3r56[1] C 6AI
1H-indazol-6-amine[10 atoms] A 88.9
/75.5 9
/9 PPIF_HUMAN Peptidyl-prolyl cis-trans isomerase F, mitochondri..

3r57[1] C N3M
N-(3-aminophenyl)acetamide[11 atoms] A 88.9
/75.5 9
/9 PPIF_HUMAN Peptidyl-prolyl cis-trans isomerase F, mitochondri..

3r57[2] D N3M
N-(3-aminophenyl)acetamide[11 atoms] A 100.0
/75.5 7
/7 PPIF_HUMAN Peptidyl-prolyl cis-trans isomerase F, mitochondri..

3r57[1] F N3M
N-(3-aminophenyl)acetamide[11 atoms] A 40.0
/75.5 5
/5 PPIF_HUMAN Peptidyl-prolyl cis-trans isomerase F, mitochondri..

3r59[1] B 3AO
1-(3-aminophenyl)ethanone[10 atoms] A 88.9
/75.5 9
/9 PPIF_HUMAN Peptidyl-prolyl cis-trans isomerase F, mitochondri..

3rcf[1] B BS4
N-[(4-aminophenyl)sulfonyl]benzamide[19 atoms] A 100.0
/75.5 9
/9 PPIF_HUMAN Peptidyl-prolyl cis-trans isomerase F, mitochondri..

3rcf[1] C BS4
N-[(4-aminophenyl)sulfonyl]benzamide[19 atoms] A 100.0
/75.5 3
/3 PPIF_HUMAN Peptidyl-prolyl cis-trans isomerase F, mitochondri..

3rci[3] B M3I
5-methyl-1,2-oxazol-3-amine[7 atoms] A 100.0
/75.5 7
/7 PPIF_HUMAN Peptidyl-prolyl cis-trans isomerase F, mitochondri..

3rci[1] E M3I
5-methyl-1,2-oxazol-3-amine[7 atoms] A 40.0
/75.5 5
/5 PPIF_HUMAN Peptidyl-prolyl cis-trans isomerase F, mitochondri..

3rck[2] B 1FP
piperazine-1-carbaldehyde[8 atoms] A 90.0
/75.5 10
/10 PPIF_HUMAN Peptidyl-prolyl cis-trans isomerase F, mitochondri..

3rck[1] D 1FP
piperazine-1-carbaldehyde[8 atoms] A 100.0
/75.5 8
/8 PPIF_HUMAN Peptidyl-prolyl cis-trans isomerase F, mitochondri..

3rck[1] E 1FP
piperazine-1-carbaldehyde[8 atoms] A 33.3
/75.5 3
/3 PPIF_HUMAN Peptidyl-prolyl cis-trans isomerase F, mitochondri..

3rck[1] F 1FP
piperazine-1-carbaldehyde[8 atoms] A 66.7
/75.5 6
/6 PPIF_HUMAN Peptidyl-prolyl cis-trans isomerase F, mitochondri..

3rcl[1] B 5AO
3-(1,3-oxazol-5-yl)aniline[12 atoms] A 88.9
/75.5 9
/9 PPIF_HUMAN Peptidyl-prolyl cis-trans isomerase F, mitochondri..

3rd9[1] B MSY
3-(3-methyl-5-oxo-4,5-dihydro-1H-pyrazol-1-yl)benz.. A 100.0
/75.5 9
/9 PPIF_HUMAN Peptidyl-prolyl cis-trans isomerase F, mitochondri..

3rda[3] B MIO
3-methyl-1,2-oxazol-5-amine[7 atoms] A 100.0
/75.5 5
/5 PPIF_HUMAN Peptidyl-prolyl cis-trans isomerase F, mitochondri..

3rda[1] E MIO
3-methyl-1,2-oxazol-5-amine[7 atoms] A 60.0
/75.5 5
/5 PPIF_HUMAN Peptidyl-prolyl cis-trans isomerase F, mitochondri..

3rda[1] F MIO
3-methyl-1,2-oxazol-5-amine[7 atoms] A 100.0
/75.5 3
/4 PPIF_HUMAN Peptidyl-prolyl cis-trans isomerase F, mitochondri..

3rda[1] G MIO
3-methyl-1,2-oxazol-5-amine[7 atoms] A 75.0
/75.5 4
/4 PPIF_HUMAN Peptidyl-prolyl cis-trans isomerase F, mitochondri..

3rda[1] H MIO
3-methyl-1,2-oxazol-5-amine[7 atoms] A 100.0
/75.5 5
/5 PPIF_HUMAN Peptidyl-prolyl cis-trans isomerase F, mitochondri..

3rdb[1] C 5MZ
3-[5-(chloromethyl)-1,2,4-oxadiazol-3-yl]aniline[1.. A 88.9
/75.5 9
/9 PPIF_HUMAN Peptidyl-prolyl cis-trans isomerase F, mitochondri..

4j58[1] B 53Z
1-(4-aminobenzyl)-3-[2-oxo-2-(pyrrolidin-1-yl)ethy.. A 92.9
/75.5 14
/14 PPIF_HUMAN Peptidyl-prolyl cis-trans isomerase F, mitochondri..

4j59[1] B 671
1-(4-aminobenzyl)-3-{2-[(2R)-2-(naphthalen-1-yl)py.. A 93.8
/75.5 16
/16 PPIF_HUMAN Peptidyl-prolyl cis-trans isomerase F, mitochondri..

4j5a[1] B 67Z
1-(4-aminobenzyl)-3-{2-[(2R)-2-(2,5-dimethoxypheny.. A 100.0
/75.5 14
/14 PPIF_HUMAN Peptidyl-prolyl cis-trans isomerase F, mitochondri..

4j5b[1] B 6B4
1-(4-aminobenzyl)-3-(2-{(2R)-2-[2-(methylsulfanyl).. A 92.3
/75.5 13
/13 PPIF_HUMAN Peptidyl-prolyl cis-trans isomerase F, mitochondri..

4j5c[2] B 7I6
1-(4-aminobenzyl)-3-[(2S)-4-(methylsulfanyl)-1-{(2.. A 93.3
/75.5 15
/15 PPIF_HUMAN Peptidyl-prolyl cis-trans isomerase F, mitochondri..

4j5d[1] B 728
1-(4-aminobenzyl)-3-{2-[(2R)-2-(2-bromophenyl)pyrr.. A 93.8
/75.5 16
/16 PPIF_HUMAN Peptidyl-prolyl cis-trans isomerase F, mitochondri..

4j5e[1] B 7B7
1-(4-aminobenzyl)-3-{2-[(2R)-2-(2-methoxyphenyl)py.. A 94.1
/75.5 17
/17 PPIF_HUMAN Peptidyl-prolyl cis-trans isomerase F, mitochondri..

5cbt[1] B 4ZL
ethyl N-(benzylcarbamoyl)glycinate[17 atoms] A 100.0
/75.5 11
/11 PPIF_HUMAN Peptidyl-prolyl cis-trans isomerase F, mitochondri..

5cbu[1] F 4ZM
ethyl N-{[3-(pyridin-4-yl)benzyl]carbamoyl}glycina.. A 85.7
/75.5 14
/14 PPIF_HUMAN Peptidyl-prolyl cis-trans isomerase F, mitochondri..

5cbu[1] G 4ZM
ethyl N-{[3-(pyridin-4-yl)benzyl]carbamoyl}glycina.. A 88.9
/75.5 9
/9 PPIF_HUMAN Peptidyl-prolyl cis-trans isomerase F, mitochondri..

5cbv[1] F 4ZP
ethyl N-{[3-(pyridin-3-yl)benzyl]carbamoyl}glycina.. A 92.9
/75.5 14
/14 PPIF_HUMAN Human Cyclophilin D

5cbw[1] G 4ZO
ethyl N-{[4-(acetylamino)benzyl]carbamoyl}glycinat.. A 85.7
/75.5 14
/14 PPIF_HUMAN Peptidyl-prolyl cis-trans isomerase F, mitochondri..

5ccn[1] G 4ZZ
ethyl N-{[3-(3-aminopyridin-4-yl)benzyl]carbamoyl}.. A 100.0
/75.5 12
/12 PPIF_HUMAN Peptidyl-prolyl cis-trans isomerase F, mitochondri..

5ccq[1] G 502
ethyl N-{[(2-aminopyridin-4-yl)methyl]carbamoyl}gl.. A 100.0
/75.5 12
/12 PPIF_HUMAN Peptidyl-prolyl cis-trans isomerase F, mitochondri..

5ccr[1] H 4ZT
ethyl N-[(4-aminobenzyl)carbamoyl]-L-methioninate[.. A 93.3
/75.5 15
/15 PPIF_HUMAN Peptidyl-prolyl cis-trans isomerase F, mitochondri..

6r8l[1] B JUZ
1-[2-[(2~{R})-2-(2-methylsulfanylphenyl)pyrrolidin.. A 94.4
/75.5 18
/18 PPIF_HUMAN Peptidyl-prolyl cis-trans isomerase F, mitochondri..

6r8o[1] E JV2
1-(((2R,3S,6R)-3-hydroxy-2,3,4,6-tetrahydro-1H-2,6.. A 88.9
/75.5 18
/18 PPIF_HUMAN Peptidyl-prolyl cis-trans isomerase F, mitochondri..

6r8w[1] B O4B
1,4,7,10,13,16-HEXAOXACYCLOOCTADECANE[18 atoms] A 60.0
/75.5 5
/5 PPIF_HUMAN Peptidyl-prolyl cis-trans isomerase F, mitochondri..

6r8w[1] D JVH
2-(exo-3,5-Dioxo-4-aza-tricyclo[5.2.1.02,6]dec-4-y.. A 88.9
/75.5 18
/18 PPIF_HUMAN Peptidyl-prolyl cis-trans isomerase F, mitochondri..

6r9s[2] B JVN
(1~{R},9~{R},10~{S})-4-fluoranyl-12-oxa-8-azatricy.. A 83.3
/75.5 12
/12 PPIF_HUMAN Peptidyl-prolyl cis-trans isomerase F, mitochondri..

6r9u[2] B JVQ
14-ethyl-4,6-dioxa-10,14-diazatricyclo[7.6.0.0^{3,.. A 83.3
/75.5 12
/12 PPIF_HUMAN Peptidyl-prolyl cis-trans isomerase F, mitochondri..

6r9x[1] B JW2
~{N}'-cyclopentyl-~{N}-(pyridin-2-ylmethyl)ethaned.. A 100.0
/75.5 12
/12 PPIF_HUMAN Peptidyl-prolyl cis-trans isomerase F, mitochondri..

6ra1[1] B JWB
2-[(1~{R},2~{R},6~{S},7~{S})-3,5-bis(oxidanylidene.. A 100.0
/75.5 9
/9 PPIF_HUMAN Peptidyl-prolyl cis-trans isomerase F, mitochondri..

6y3e[1] G 12P
DODECAETHYLENE GLYCOL[16 atoms] A 50.0
/75.5 4
/4 PPIF_HUMAN Peptidyl-prolyl cis-trans isomerase F, mitochondri..

6y3e[1] H 12P
DODECAETHYLENE GLYCOL[10 atoms] A 60.0
/75.5 5
/5 PPIF_HUMAN Peptidyl-prolyl cis-trans isomerase F, mitochondri..

7ogi[1] B VDH
N-(5-ethyl-4-oxidanylidene-1,2,3,6-tetrahydro-1,5-.. A 84.6
/75.5 13
/13 PPIF_HUMAN Peptidyl-prolyl cis-trans isomerase F, mitochondri..

7pmt[1] C 7UO
~{N}-[(5-ethyl-4-oxidanylidene-1,2,3,6-tetrahydro-.. A 82.4
/75.5 17
/17 PPIF_HUMAN Peptidyl-prolyl cis-trans isomerase F, mitochondri..

7r2i[1] C UPZ
ethyl 7-methyl-2-oxidanylidene-1,3-dihydropyrazolo.. A 88.9
/75.5 9
/9 PPIF_HUMAN Peptidyl-prolyl cis-trans isomerase F, mitochondri..

7r2j[1] B V0Z
N-(4-aminophenyl)-7-methyl-2-oxo-1H,2H-pyrazolo[1,.. A 81.8
/75.5 11
/11 PPIF_HUMAN Peptidyl-prolyl cis-trans isomerase F, mitochondri..

7r2l[1] B UX5
N-(4-aminophenyl)-7-methyl-2-oxo-1H,2H-pyrazolo[1,.. A 84.6
/75.5 13
/13 PPIF_HUMAN Peptidyl-prolyl cis-trans isomerase F, mitochondri..

7tgs[1] B I3Q
(4S,7R,11S,13E,19S)-N-[2-(2-aminoethoxy)ethyl]-4-[.. A 92.9
/75.5 14
/14 PPIF_HUMAN Peptidyl-prolyl cis-trans isomerase F, mitochondri..

7tgt[1] B I4F
(4S,7S,11R,13E,19S)-N-[2-(2-aminoethoxy)ethyl]-7-b.. A 93.8
/75.5 16
/16 PPIF_HUMAN Peptidyl-prolyl cis-trans isomerase F, mitochondri..

7tgv[1] B I3X
(4S,7S,11R,13E,19S)-N-[2-(2-aminoethoxy)ethyl]-7-b.. A 90.5
/75.5 21
/21 PPIF_HUMAN Peptidyl-prolyl cis-trans isomerase F, mitochondri..

7th1[1] B I5J
(4S,7S,11R,13E,19S)-N-[2-(2-aminoethoxy)ethyl]-7-b.. A 88.9
/75.5 18
/18 PPIF_HUMAN Peptidyl-prolyl cis-trans isomerase F, mitochondri..

7th6[1] B I56
4'-{[(4S,7S,11R,13E,19S)-19-{[2-(2-aminoethoxy)eth.. A 85.0
/75.5 20
/20 PPIF_HUMAN Peptidyl-prolyl cis-trans isomerase F, mitochondri..

7th7[1] B I5E
3-(4'-{[(4S,7S,11R,19S)-19-{[2-(2-aminoethoxy)ethy.. A 91.7
/75.5 24
/24 PPIF_HUMAN Peptidyl-prolyl cis-trans isomerase F, mitochondri..

7thc[1] B I4Z
3-(4'-{[(4S,7S,11R,13E,19S)-19-{[2-(2-aminoethoxy).. A 91.3
/75.5 23
/23 PPIF_HUMAN Peptidyl-prolyl cis-trans isomerase F, mitochondri..

7thd[1] B I4V
[(4'-{[(4S,7S,11R,13E,19S)-19-{[2-(2-aminoethoxy)e.. A 91.7
/75.5 24
/24 PPIF_HUMAN Peptidyl-prolyl cis-trans isomerase F, mitochondri..

7thf[1] B I4R
3-(4'-{[(4S,7S,11R,13E,19S)-19-{[2-(2-aminoethoxy).. A 91.3
/75.5 23
/23 PPIF_HUMAN Peptidyl-prolyl cis-trans isomerase F, mitochondri..

8uc4[1] B 15P
POLYETHYLENE GLYCOL (N=34)[11 atoms] A 33.3
/75.5 3
/3 PPIF_HUMAN Peptidyl-prolyl cis-trans isomerase F, mitochondri..

8uc4[1] E 15P
POLYETHYLENE GLYCOL (N=34)[15 atoms] A 75.0
/75.5 4
/4 PPIF_HUMAN Peptidyl-prolyl cis-trans isomerase F, mitochondri..

8ejx[1] B 9JT
N-phenyl-2-selanylbenzamide[16 atoms] A 100.0
/75.3 9
/9 PPIF_HUMAN Peptidyl-prolyl cis-trans isomerase F, mitochondri..

5ccs[1] B C4Y
1-(4-aminobenzyl)-3-{2-oxo-2-[(2R)-2-phenylpyrroli.. A 100.0
/74.8 14
/14 PPIF_HUMAN Peptidyl-prolyl cis-trans isomerase F, mitochondri..

7zdn[2] C IU0
(1~{R},9~{R},10~{S})-12-oxa-8-azatricyclo[7.3.1.0^.. A 83.3
/74.8 12
/12 PPIF_HUMAN Peptidyl-prolyl cis-trans isomerase F, mitochondri..

1e3b[1] C 3EP
TRIETHYLPHOSPHANE[7 atoms] A 100.0
/70.3 2
/2 CYP3_CAEEL CYCLOPHILIN 3

4fru[2] D ME2
1-ETHOXY-2-(2-METHOXYETHOXY)ETHANE[10 atoms] A 40.0
/64.0 5
/5 A5YBL8_HORSE Peptidyl-prolyl cis-trans isomerase

3.a³:asym_id for the contact molecule. 4.a⁴:asym_id for the template homologue. 5.identity[%]⁵:sequence identity between the query and the template homologue only for the contact residues. Number after the slash / is sequence identity for all the aligned region. 6.Ncon⁶:number of aligned contact residues for the query. Number after the slash / is number of contact residues in the template homologue.

METAL

165 pdb_id contact mol homologue

a³ description a⁴ identity[%]⁵ Ncon⁶ description

2wfj[1] F CL
CHLORIDE ION[1 atoms] A 83.3
/56.6 6
/6 PPIG_HUMAN PEPTIDYL-PROLYL CIS-TRANS ISOMERASE G

3rcg[1] C CL
CHLORIDE ION[1 atoms] A 100.0
/75.5 1
/1 PPIF_HUMAN Peptidyl-prolyl cis-trans isomerase F, mitochondri..

4i9y[3] AA CL
CHLORIDE ION[1 atoms] D 100.0
/66.5 1
/2 RBP2_HUMAN E3 SUMO-protein ligase RanBP2

4ipz[1] C CL
CHLORIDE ION[1 atoms] A 100.0
/100.0 1
/1 PPIA_HUMAN Peptidyl-prolyl cis-trans isomerase A

4ipz[1] D CL
CHLORIDE ION[1 atoms] A 100.0
/100.0 2
/2 PPIA_HUMAN Peptidyl-prolyl cis-trans isomerase A

4jcp[1] F CL
CHLORIDE ION[1 atoms] A 100.0
/75.8 2
/2 A8QGU4_BRUMA Peptidyl-prolyl cis-trans isomerase

5hsv[1] I CL
CHLORIDE ION[1 atoms] A 100.0
/100.0 3
/3 PPIA_CHLAE Peptidyl-prolyl cis-trans isomerase A

5hsv[1] J CL
CHLORIDE ION[1 atoms] B 100.0
/100.0 3
/3 PPIA_CHLAE Peptidyl-prolyl cis-trans isomerase A

5hsv[1] K CL
CHLORIDE ION[1 atoms] B 100.0
/100.0 2
/2 PPIA_CHLAE Peptidyl-prolyl cis-trans isomerase A

5hsv[1] L CL
CHLORIDE ION[1 atoms] C 100.0
/100.0 6
/6 PPIA_CHLAE Peptidyl-prolyl cis-trans isomerase A

3r57[1] B NA
SODIUM ION[1 atoms] A 50.0
/75.5 2
/2 PPIF_HUMAN Peptidyl-prolyl cis-trans isomerase F, mitochondri..

4eyv[1] E NA
SODIUM ION[1 atoms] A 16.7
/62.7 6
/6 C6KGV3_PIRIN Peptidyl-prolyl cis-trans isomerase

4eyv[2] F NA
SODIUM ION[1 atoms] A 80.0
/62.7 5
/5 C6KGV3_PIRIN Peptidyl-prolyl cis-trans isomerase

4eyv[1] G NA
SODIUM ION[1 atoms] A 37.5
/62.7 8
/8 C6KGV3_PIRIN Peptidyl-prolyl cis-trans isomerase

4eyv[1] H NA
SODIUM ION[1 atoms] A 66.7
/62.7 3
/3 C6KGV3_PIRIN Peptidyl-prolyl cis-trans isomerase

4eyv[1] K NA
SODIUM ION[1 atoms] B 28.6
/62.7 7
/7 C6KGV3_PIRIN Peptidyl-prolyl cis-trans isomerase

4eyv[1] M NA
SODIUM ION[1 atoms] B 100.0
/62.7 6
/6 C6KGV3_PIRIN Peptidyl-prolyl cis-trans isomerase

4eyv[2] N NA
SODIUM ION[1 atoms] B 85.7
/62.7 7
/7 C6KGV3_PIRIN Peptidyl-prolyl cis-trans isomerase

4eyv[1] R NA
SODIUM ION[1 atoms] C 25.0
/62.7 4
/4 C6KGV3_PIRIN Peptidyl-prolyl cis-trans isomerase

6y3e[1] K NA
SODIUM ION[1 atoms] A 100.0
/75.5 1
/1 PPIF_HUMAN Peptidyl-prolyl cis-trans isomerase F, mitochondri..

4eyv[3] D K
POTASSIUM ION[1 atoms] A 0.0
/62.7 5
/5 C6KGV3_PIRIN Peptidyl-prolyl cis-trans isomerase

4eyv[1] O K
POTASSIUM ION[1 atoms] C 50.0
/62.7 2
/2 C6KGV3_PIRIN Peptidyl-prolyl cis-trans isomerase

5cbt[3] D K
POTASSIUM ION[1 atoms] A 66.7
/75.5 3
/3 PPIF_HUMAN Peptidyl-prolyl cis-trans isomerase F, mitochondri..

2alf[1] B MG
MAGNESIUM ION[1 atoms] A 100.0
/98.8 7
/7 PPIA_HUMAN Peptidyl-prolyl cis-trans isomerase A

6hmz[1] C MG
MAGNESIUM ION[1 atoms] A 100.0
/74.1 4
/5 A0A078GRH6_BRANA Peptidyl-prolyl cis-trans isomerase

1e3b[1] B AU
GOLD ION[1 atoms] A 100.0
/70.3 2
/2 CYP3_CAEEL CYCLOPHILIN 3

2esl[6] N ZN
ZINC ION[1 atoms] A 0.0
/63.4 1
/1 PPIC_HUMAN Peptidyl-prolyl cis-trans isomerase C

4fru[2] B ZN
ZINC ION[1 atoms] A 100.0
/64.0 2
/2 A5YBL8_HORSE Peptidyl-prolyl cis-trans isomerase

4fru[2] C ZN
ZINC ION[1 atoms] A 0.0
/64.0 1
/1 A5YBL8_HORSE Peptidyl-prolyl cis-trans isomerase

2esl[6] M CA
CALCIUM ION[1 atoms] A 0.0
/63.4 1
/1 PPIC_HUMAN Peptidyl-prolyl cis-trans isomerase C

2esl[1] V CA
CALCIUM ION[1 atoms] F 100.0
/63.4 2
/2 PPIC_HUMAN Peptidyl-prolyl cis-trans isomerase C

2gw2[1] B UNX
UNKNOWN ATOM OR ION[1 atoms] A 0.0
/55.3 1
/1 PPIG_HUMAN Peptidyl-prolyl cis-trans isomerase G

2gw2[1] C UNX
UNKNOWN ATOM OR ION[1 atoms] A 60.0
/55.3 5
/6 PPIG_HUMAN Peptidyl-prolyl cis-trans isomerase G

2gw2[1] D UNX
UNKNOWN ATOM OR ION[1 atoms] A 100.0
/55.3 3
/3 PPIG_HUMAN Peptidyl-prolyl cis-trans isomerase G

2gw2[1] E UNX
UNKNOWN ATOM OR ION[1 atoms] A 66.7
/55.3 3
/3 PPIG_HUMAN Peptidyl-prolyl cis-trans isomerase G

3.a³:asym_id for the contact molecule. 4.a⁴:asym_id for the template homologue. 5.identity[%]⁵:sequence identity between the query and the template homologue only for the contact residues. Number after the slash / is sequence identity for all the aligned region. 6.Ncon⁶:number of aligned contact residues for the query. Number after the slash / is number of contact residues in the template homologue.

OTHERPOLY

165 pdb_id contact mol homologue

a³ description a⁴ identity[%]⁵ Ncon⁶ description

7pcj[2] B Cyclosporin A A 100.0
/99.4 13
/13 PPIA_HUMAN Peptidyl-prolyl cis-trans isomerase A

3.a³:asym_id for the contact molecule. 4.a⁴:asym_id for the template homologue. 5.identity[%]⁵:sequence identity between the query and the template homologue only for the contact residues. Number after the slash / is sequence identity for all the aligned region. 6.Ncon⁶:number of aligned contact residues for the query. Number after the slash / is number of contact residues in the template homologue.

HOMO

165 pdb_id contact mol homologue

a³ description a⁴ identity[%]⁵ Ncon⁶ description

1rmh[34] B CYPH_HUMAN CYCLOPHILIN A[164 aa] A 100.0
/100.0 4
/4 CYPH_HUMAN CYCLOPHILIN A

2rma[30] C PPIA_HUMAN PEPTIDYL-PROLYL CIS-TRANS ISOMERASE[165 aa] A 100.0
/100.0 6
/6 PPIA_HUMAN PEPTIDYL-PROLYL CIS-TRANS ISOMERASE

2rma[30] K PPIA_HUMAN PEPTIDYL-PROLYL CIS-TRANS ISOMERASE[165 aa] A 100.0
/100.0 1
/1 PPIA_HUMAN PEPTIDYL-PROLYL CIS-TRANS ISOMERASE

2rma[30] M PPIA_HUMAN PEPTIDYL-PROLYL CIS-TRANS ISOMERASE[165 aa] A 100.0
/100.0 6
/6 PPIA_HUMAN PEPTIDYL-PROLYL CIS-TRANS ISOMERASE

2x2a[2] B PPIA_HUMAN PEPTIDYL-PROLYL CIS-TRANS ISOMERASE A[164 aa] A 96.0
/99.4 25
/25 PPIA_HUMAN PEPTIDYL-PROLYL CIS-TRANS ISOMERASE A

6ybm[2] B PPIF_HUMAN Peptidyl-prolyl cis-trans isomerase F, mitochondri.. A 72.7
/75.5 11
/11 PPIF_HUMAN Peptidyl-prolyl cis-trans isomerase F, mitochondri..

6ybm[2] C PPIF_HUMAN Peptidyl-prolyl cis-trans isomerase F, mitochondri.. A 100.0
/75.5 1
/1 PPIF_HUMAN Peptidyl-prolyl cis-trans isomerase F, mitochondri..

6ybm[1] C PPIF_HUMAN Peptidyl-prolyl cis-trans isomerase F, mitochondri.. B 80.0
/75.5 10
/10 PPIF_HUMAN Peptidyl-prolyl cis-trans isomerase F, mitochondri..

6ybm[1] B PPIF_HUMAN Peptidyl-prolyl cis-trans isomerase F, mitochondri.. C 54.5
/75.5 11
/11 PPIF_HUMAN Peptidyl-prolyl cis-trans isomerase F, mitochondri..

3uch[3] A PPIE_HUMAN Peptidyl-prolyl cis-trans isomerase E[173 aa] A 82.4
/67.7 17
/17 PPIE_HUMAN Peptidyl-prolyl cis-trans isomerase E

3uch[3] A PPIE_HUMAN Peptidyl-prolyl cis-trans isomerase E[173 aa] A 50.0
/67.7 4
/12 PPIE_HUMAN Peptidyl-prolyl cis-trans isomerase E

5yb9[4] A A2DT06_TRIVA Peptidyl-prolyl cis-trans isomerase[172 aa] A 35.7
/65.2 14
/18 A2DT06_TRIVA Peptidyl-prolyl cis-trans isomerase

1iip[4] A PPID_BOVIN Cyclophilin 40[297 aa] A 40.0
/63.8 5
/5 PPID_BOVIN Cyclophilin 40

2esl[6] B PPIC_HUMAN Peptidyl-prolyl cis-trans isomerase C[181 aa] A 50.0
/63.4 8
/12 PPIC_HUMAN Peptidyl-prolyl cis-trans isomerase C

2esl[6] C PPIC_HUMAN Peptidyl-prolyl cis-trans isomerase C[181 aa] A 0.0
/63.4 3
/9 PPIC_HUMAN Peptidyl-prolyl cis-trans isomerase C

2esl[6] D PPIC_HUMAN Peptidyl-prolyl cis-trans isomerase C[181 aa] A 0.0
/63.4 1
/1 PPIC_HUMAN Peptidyl-prolyl cis-trans isomerase C

3.a³:asym_id for the contact molecule. 4.a⁴:asym_id for the template homologue. 5.identity[%]⁵:sequence identity between the query and the template homologue only for the contact residues. Number after the slash / is sequence identity for all the aligned region. 6.Ncon⁶:number of aligned contact residues for the query. Number after the slash / is number of contact residues in the template homologue.

PRECIPITANT

165 pdb_id contact mol homologue

a³ description a⁴ identity[%]⁵ Ncon⁶ description

1e8k[1] B ALA
ALANINE[5 atoms] A 100.0
/70.3 3
/3 CYP3_CAEEL PEPTIDYL-PROLYL CIS-TRANS ISOMERASE 3

2cfe[2] B ALA
ALANINE[5 atoms] A 100.0
/71.3 3
/3 O93970_9BASI ALLERGEN

1iip[4] B GOL
GLYCEROL[6 atoms] A 0.0
/63.8 2
/5 PPID_BOVIN Cyclophilin 40

2cfe[4] D GOL
GLYCEROL[6 atoms] A 42.9
/71.3 7
/7 O93970_9BASI ALLERGEN

2x2a[1] C GOL
GLYCEROL[6 atoms] A 100.0
/99.4 2
/2 PPIA_HUMAN PEPTIDYL-PROLYL CIS-TRANS ISOMERASE A

2xgy[1] D GOL
GLYCEROL[6 atoms] B 100.0
/100.0 3
/3 PPIA_HUMAN PEPTIDYL-PROLYL CIS-TRANS ISOMERASE A

3r4g[1] D GOL
GLYCEROL[6 atoms] A 100.0
/75.5 5
/5 PPIF_HUMAN Peptidyl-prolyl cis-trans isomerase F, mitochondri..

3r4g[1] E GOL
GLYCEROL[6 atoms] A 100.0
/75.5 1
/1 PPIF_HUMAN Peptidyl-prolyl cis-trans isomerase F, mitochondri..

3r4g[1] F GOL
GLYCEROL[6 atoms] A 100.0
/75.5 7
/7 PPIF_HUMAN Peptidyl-prolyl cis-trans isomerase F, mitochondri..

3r57[1] G GOL
GLYCEROL[6 atoms] A 0.0
/75.5 2
/2 PPIF_HUMAN Peptidyl-prolyl cis-trans isomerase F, mitochondri..

3r57[3] H GOL
GLYCEROL[6 atoms] A 75.0
/75.5 4
/4 PPIF_HUMAN Peptidyl-prolyl cis-trans isomerase F, mitochondri..

4i9y[5] G GOL
GLYCEROL[6 atoms] A 87.5
/66.5 8
/8 RBP2_HUMAN E3 SUMO-protein ligase RanBP2

4i9y[6] H GOL
GLYCEROL[6 atoms] A 0.0
/66.5 2
/3 RBP2_HUMAN E3 SUMO-protein ligase RanBP2

4i9y[6] K GOL
GLYCEROL[6 atoms] A 100.0
/66.5 2
/4 RBP2_HUMAN E3 SUMO-protein ligase RanBP2

4i9y[2] M GOL
GLYCEROL[6 atoms] B 66.7
/66.5 3
/3 RBP2_HUMAN E3 SUMO-protein ligase RanBP2

4i9y[1] N GOL
GLYCEROL[6 atoms] B 100.0
/66.5 1
/1 RBP2_HUMAN E3 SUMO-protein ligase RanBP2

6gji[2] C GOL
GLYCEROL[6 atoms] A 100.0
/100.0 4
/4 PPIA_HUMAN Peptidyl-prolyl cis-trans isomerase A

6lxo[2] H GOL
GLYCEROL[6 atoms] A 75.0
/65.0 4
/4 A2DLL4_TRIVA Peptidyl-prolyl cis-trans isomerase

6lxq[6] I GOL
GLYCEROL[6 atoms] A 66.7
/65.0 3
/3 A2DLL4_TRIVA Peptidyl-prolyl cis-trans isomerase

2igv[1] B SER
SERINE[6 atoms] A 100.0
/70.3 3
/3 CYP3_CAEEL Peptidyl-prolyl cis-trans isomerase 3

3cyh[1] B SER
SERINE[6 atoms] A 100.0
/100.0 3
/3 CYPH_HUMAN CYCLOPHILIN A

2igw[1] B GLY
GLYCINE[4 atoms] A 100.0
/70.3 3
/3 CYP3_CAEEL Peptidyl-prolyl cis-trans isomerase 3

4n1m[1] B GLY
GLYCINE[4 atoms] A 100.0
/100.0 4
/4 PPIA_HUMAN Peptidyl-prolyl cis-trans isomerase A

5cyh[1] B GLY
GLYCINE[4 atoms] A 100.0
/100.0 4
/4 CYPH_HUMAN CYCLOPHILIN A

2wfj[1] C EDO
1,2-ETHANEDIOL[3 atoms] A 0.0
/56.6 2
/2 PPIG_HUMAN PEPTIDYL-PROLYL CIS-TRANS ISOMERASE G

3k2c[2] F EDO
1,2-ETHANEDIOL[4 atoms] A 50.0
/64.2 2
/2 CYPH_ENCCU Peptidyl-prolyl cis-trans isomerase

5cbt[1] G EDO
1,2-ETHANEDIOL[4 atoms] A 66.7
/75.5 3
/3 PPIF_HUMAN Peptidyl-prolyl cis-trans isomerase F, mitochondri..

5cbu[2] D EDO
1,2-ETHANEDIOL[4 atoms] A 100.0
/75.5 3
/3 PPIF_HUMAN Peptidyl-prolyl cis-trans isomerase F, mitochondri..

6fk1[2] B EDO
1,2-ETHANEDIOL[4 atoms] A 100.0
/96.3 5
/5 PPIA_MOUSE Peptidyl-prolyl cis-trans isomerase A

6fk1[7] C EDO
1,2-ETHANEDIOL[4 atoms] A 100.0
/96.3 3
/3 PPIA_MOUSE Peptidyl-prolyl cis-trans isomerase A

6y3e[3] B EDO
1,2-ETHANEDIOL[4 atoms] A 33.3
/75.5 3
/3 PPIF_HUMAN Peptidyl-prolyl cis-trans isomerase F, mitochondri..

6y3e[1] F EDO
1,2-ETHANEDIOL[4 atoms] A 75.0
/75.5 4
/4 PPIF_HUMAN Peptidyl-prolyl cis-trans isomerase F, mitochondri..

6ybm[2] F EDO
1,2-ETHANEDIOL[4 atoms] A 75.0
/75.5 4
/4 PPIF_HUMAN Peptidyl-prolyl cis-trans isomerase F, mitochondri..

6ybm[1] F EDO
1,2-ETHANEDIOL[4 atoms] B 100.0
/75.5 1
/1 PPIF_HUMAN Peptidyl-prolyl cis-trans isomerase F, mitochondri..

6ybm[2] G EDO
1,2-ETHANEDIOL[4 atoms] C 75.0
/75.5 4
/4 PPIF_HUMAN Peptidyl-prolyl cis-trans isomerase F, mitochondri..

7uxm[1] H EDO
1,2-ETHANEDIOL[4 atoms] B 100.0
/100.0 4
/4 PPIA_HUMAN Peptidyl-prolyl cis-trans isomerase A

7uxm[1] I EDO
1,2-ETHANEDIOL[4 atoms] B 100.0
/100.0 3
/3 PPIA_HUMAN Peptidyl-prolyl cis-trans isomerase A

7uxm[1] L EDO
1,2-ETHANEDIOL[4 atoms] B 100.0
/100.0 1
/1 PPIA_HUMAN Peptidyl-prolyl cis-trans isomerase A

7uxm[1] M EDO
1,2-ETHANEDIOL[4 atoms] C 100.0
/100.0 5
/5 PPIA_HUMAN Peptidyl-prolyl cis-trans isomerase A

7uxm[1] O EDO
1,2-ETHANEDIOL[4 atoms] C 100.0
/100.0 5
/5 PPIA_HUMAN Peptidyl-prolyl cis-trans isomerase A

7uxm[2] Q EDO
1,2-ETHANEDIOL[4 atoms] C 100.0
/100.0 4
/4 PPIA_HUMAN Peptidyl-prolyl cis-trans isomerase A

7uxm[1] R EDO
1,2-ETHANEDIOL[4 atoms] C 100.0
/100.0 4
/4 PPIA_HUMAN Peptidyl-prolyl cis-trans isomerase A

8cu5[1] D EDO
1,2-ETHANEDIOL[4 atoms] A 100.0
/63.2 4
/4 Q6YNZ2_BRUMA Peptidyl-prolyl cis-trans isomerase

8cu5[3] E EDO
1,2-ETHANEDIOL[4 atoms] A 100.0
/63.2 4
/4 Q6YNZ2_BRUMA Peptidyl-prolyl cis-trans isomerase

8cu5[1] F EDO
1,2-ETHANEDIOL[4 atoms] A 50.0
/63.2 4
/4 Q6YNZ2_BRUMA Peptidyl-prolyl cis-trans isomerase

5cbt[6] E FMT
FORMIC ACID[3 atoms] A 80.0
/75.5 5
/5 PPIF_HUMAN Peptidyl-prolyl cis-trans isomerase F, mitochondri..

6gjn[1] C FMT
FORMIC ACID[3 atoms] A 100.0
/100.0 2
/2 PPIA_HUMAN Peptidyl-prolyl cis-trans isomerase A

6gjn[1] D FMT
FORMIC ACID[3 atoms] A 100.0
/100.0 1
/1 PPIA_HUMAN Peptidyl-prolyl cis-trans isomerase A

5nou[1] E TRS
2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL[8 atoms] A 100.0
/100.0 2
/2 PPIA_HUMAN Peptidyl-prolyl cis-trans isomerase A

2biu[1] B DMS
DIMETHYL SULFOXIDE[4 atoms] A 100.0
/75.5 4
/4 PPIF_HUMAN PEPTIDYL-PROLYL CIS-TRANS ISOMERASE

2biu[8] C DMS
DIMETHYL SULFOXIDE[4 atoms] A 100.0
/75.5 8
/8 PPIF_HUMAN PEPTIDYL-PROLYL CIS-TRANS ISOMERASE

2biu[1] E DMS
DIMETHYL SULFOXIDE[4 atoms] A 60.0
/75.5 5
/5 PPIF_HUMAN PEPTIDYL-PROLYL CIS-TRANS ISOMERASE

4j5a[1] C DMS
DIMETHYL SULFOXIDE[4 atoms] A 80.0
/75.5 5
/5 PPIF_HUMAN Peptidyl-prolyl cis-trans isomerase F, mitochondri..

6gs6[1] C DMS
DIMETHYL SULFOXIDE[4 atoms] A 100.0
/99.4 3
/3 PPIA_HUMAN Peptidyl-prolyl cis-trans isomerase A

2z6w[1] E CIT
CITRIC ACID[13 atoms] A 80.0
/75.5 5
/5 PPIF_HUMAN PEPTIDYL-PROLYL CIS-TRANS ISOMERASE

6ybm[2] E CIT
CITRIC ACID[13 atoms] A 50.0
/75.5 2
/2 PPIF_HUMAN Peptidyl-prolyl cis-trans isomerase F, mitochondri..

6ybm[1] E CIT
CITRIC ACID[13 atoms] B 100.0
/75.5 1
/1 PPIF_HUMAN Peptidyl-prolyl cis-trans isomerase F, mitochondri..

3r56[1] B P33
3,6,9,12,15,18-HEXAOXAICOSANE-1,20-DIOL[22 atoms] A 40.0
/75.5 5
/5 PPIF_HUMAN Peptidyl-prolyl cis-trans isomerase F, mitochondri..

3rcg[1] B DMF
DIMETHYLFORMAMIDE[5 atoms] A 100.0
/75.5 8
/8 PPIF_HUMAN Peptidyl-prolyl cis-trans isomerase F, mitochondri..

3rcl[2] C P4C
O-ACETALDEHYDYL-HEXAETHYLENE GLYCOL[22 atoms] A 40.0
/75.5 5
/5 PPIF_HUMAN Peptidyl-prolyl cis-trans isomerase F, mitochondri..

3rd9[4] C PEG
DI(HYDROXYETHYL)ETHER[7 atoms] A 50.0
/75.5 2
/2 PPIF_HUMAN Peptidyl-prolyl cis-trans isomerase F, mitochondri..

4fru[3] E PEG
DI(HYDROXYETHYL)ETHER[5 atoms] A 100.0
/64.0 1
/1 A5YBL8_HORSE Peptidyl-prolyl cis-trans isomerase

5ccr[1] I PEG
DI(HYDROXYETHYL)ETHER[7 atoms] A 100.0
/75.5 3
/3 PPIF_HUMAN Peptidyl-prolyl cis-trans isomerase F, mitochondri..

8uc4[1] D PEG
DI(HYDROXYETHYL)ETHER[7 atoms] A 75.0
/75.5 4
/4 PPIF_HUMAN Peptidyl-prolyl cis-trans isomerase F, mitochondri..

4eyv[2] I PO4
PHOSPHATE ION[5 atoms] B 50.0
/62.7 2
/2 C6KGV3_PIRIN Peptidyl-prolyl cis-trans isomerase

4j58[1] C PO4
PHOSPHATE ION[5 atoms] A 100.0
/75.5 3
/3 PPIF_HUMAN Peptidyl-prolyl cis-trans isomerase F, mitochondri..

6lxq[1] C PO4
PHOSPHATE ION[5 atoms] A 33.3
/65.0 3
/3 A2DLL4_TRIVA Peptidyl-prolyl cis-trans isomerase

6lxq[1] E PO4
PHOSPHATE ION[5 atoms] A 25.0
/65.0 4
/4 A2DLL4_TRIVA Peptidyl-prolyl cis-trans isomerase

6lxq[1] F PO4
PHOSPHATE ION[5 atoms] A 33.3
/65.0 3
/3 A2DLL4_TRIVA Peptidyl-prolyl cis-trans isomerase

6r8o[2] D PO4
PHOSPHATE ION[5 atoms] A 50.0
/75.5 2
/2 PPIF_HUMAN Peptidyl-prolyl cis-trans isomerase F, mitochondri..

4o8h[3] C 1PE
PENTAETHYLENE GLYCOL[16 atoms] A 50.0
/75.5 4
/4 PPIF_HUMAN Peptidyl-prolyl cis-trans isomerase F, mitochondri..

6r9s[1] D 1PE
PENTAETHYLENE GLYCOL[16 atoms] A 90.0
/75.5 10
/10 PPIF_HUMAN Peptidyl-prolyl cis-trans isomerase F, mitochondri..

4tot[5] I P6G
HEXAETHYLENE GLYCOL[19 atoms] A 50.0
/76.7 4
/4 PPIF_RAT Peptidyl-prolyl cis-trans isomerase F, mitochondri..

5cbt[12] F PG4
TETRAETHYLENE GLYCOL[13 atoms] A 50.0
/75.5 4
/4 PPIF_HUMAN Peptidyl-prolyl cis-trans isomerase F, mitochondri..

6ra1[1] E PG4
TETRAETHYLENE GLYCOL[13 atoms] A 100.0
/75.5 6
/6 PPIF_HUMAN Peptidyl-prolyl cis-trans isomerase F, mitochondri..

5cbt[9] H PGE
TRIETHYLENE GLYCOL[10 atoms] A 75.0
/75.5 4
/4 PPIF_HUMAN Peptidyl-prolyl cis-trans isomerase F, mitochondri..

5ccr[1] G PGE
TRIETHYLENE GLYCOL[10 atoms] A 50.0
/75.5 2
/2 PPIF_HUMAN Peptidyl-prolyl cis-trans isomerase F, mitochondri..

6r9u[1] F PGE
TRIETHYLENE GLYCOL[10 atoms] A 60.0
/75.5 5
/5 PPIF_HUMAN Peptidyl-prolyl cis-trans isomerase F, mitochondri..

6hmz[1] D MLI
MALONATE ION[7 atoms] A 50.0
/74.1 2
/2 A0A078GRH6_BRANA Peptidyl-prolyl cis-trans isomerase

4i9y[3] J TLA
L(+)-TARTARIC ACID[10 atoms] A 33.3
/66.5 3
/5 RBP2_HUMAN E3 SUMO-protein ligase RanBP2

3ici[1] E MES
2-(N-MORPHOLINO)-ETHANESULFONIC ACID[12 atoms] A 100.0
/65.6 3
/3 PPIB_HUMAN Peptidyl-prolyl cis-trans isomerase B

2ck1[2] B ACT
ACETATE ION[4 atoms] A 0.0
/64.6 3
/3 PPIE_SCHMA PEPTIDYL-PROLYL CIS-TRANS ISOMERASE E

3k2c[2] E PG5
1-METHOXY-2-[2-(2-METHOXY-ETHOXY]-ETHANE[12 atoms].. A 80.0
/64.2 5
/5 CYPH_ENCCU Peptidyl-prolyl cis-trans isomerase

2esl[13] O SO4
SULFATE ION[5 atoms] A 50.0
/63.4 4
/4 PPIC_HUMAN Peptidyl-prolyl cis-trans isomerase C

2he9[1] C SO4
SULFATE ION[5 atoms] A 100.0
/52.5 3
/3 NKTR_HUMAN NK-tumor recognition protein

3k2c[2] I SO4
SULFATE ION[5 atoms] C 100.0
/64.2 2
/2 CYPH_ENCCU Peptidyl-prolyl cis-trans isomerase

4jcp[1] B SO4
SULFATE ION[5 atoms] A 100.0
/75.8 4
/5 A8QGU4_BRUMA Peptidyl-prolyl cis-trans isomerase

4jcp[1] C SO4
SULFATE ION[5 atoms] A 100.0
/75.8 1
/2 A8QGU4_BRUMA Peptidyl-prolyl cis-trans isomerase

4jcp[1] D SO4
SULFATE ION[5 atoms] A 0.0
/75.8 2
/3 A8QGU4_BRUMA Peptidyl-prolyl cis-trans isomerase

4jcp[1] E SO4
SULFATE ION[5 atoms] A 33.3
/75.8 3
/3 A8QGU4_BRUMA Peptidyl-prolyl cis-trans isomerase

6lxo[1] D SO4
SULFATE ION[5 atoms] A 33.3
/65.0 3
/3 A2DLL4_TRIVA Peptidyl-prolyl cis-trans isomerase

6lxo[1] E SO4
SULFATE ION[5 atoms] A 75.0
/65.0 4
/4 A2DLL4_TRIVA Peptidyl-prolyl cis-trans isomerase

6lxo[1] F SO4
SULFATE ION[5 atoms] A 100.0
/65.0 1
/2 A2DLL4_TRIVA Peptidyl-prolyl cis-trans isomerase

6lxo[1] G SO4
SULFATE ION[5 atoms] A 50.0
/65.0 2
/2 A2DLL4_TRIVA Peptidyl-prolyl cis-trans isomerase

6r8o[3] C SO4
SULFATE ION[5 atoms] A 75.0
/75.5 4
/4 PPIF_HUMAN Peptidyl-prolyl cis-trans isomerase F, mitochondri..

6ra1[1] G SO4
SULFATE ION[5 atoms] A 100.0
/75.5 4
/4 PPIF_HUMAN Peptidyl-prolyl cis-trans isomerase F, mitochondri..

8cu5[3] G SO4
SULFATE ION[5 atoms] A 60.0
/63.2 5
/5 Q6YNZ2_BRUMA Peptidyl-prolyl cis-trans isomerase

1h0p[1] B DTT
2,3-DIHYDROXY-1,4-DITHIOBUTANE[8 atoms] A 80.0
/58.3 5
/5 CYP5_CAEEL PEPTIDYL-PROLYL CIS-TRANS ISOMERASE 5

3.a³:asym_id for the contact molecule. 4.a⁴:asym_id for the template homologue. 5.identity[%]⁵:sequence identity between the query and the template homologue only for the contact residues. Number after the slash / is sequence identity for all the aligned region. 6.Ncon⁶:number of aligned contact residues for the query. Number after the slash / is number of contact residues in the template homologue.

MONOMER
165
	pdb_id	a¹	identity[%]²	description
	8g9p	D	100.0	PPIA_HUMAN Peptidyl-prolyl cis-trans isomerase A
	1.a¹:asym_id for the homologue. 2.identity[%]²:sequence identity between the query and the homologue.

Contact Molecules for Homologous Proteins

Summary Bars[0.0 %]

UniProt Feature Tables [P62937(PPIA_HUMAN)]