Contact Molecules for Homologous Proteins

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PID QueryLength Homolgous Sequence in PDB UniProt Query TITLE
3923226 794 284 P09958(FURIN_HUMAN) RecName: Full=Furin ; EC=3.4.21.75 ;AltName: Full=Dibasic-processing enzyme;AltName: Full=Paired basic amino acid residue-cleaving enzyme; Short=PACE;Flags: Precursor;
QUERYSEQ 
MELRPWLLWVVAATGTLVLLAADAQGQKVFTNTWAVRIPGGPAVANSVARKHGFLNLGQIFGDYYHFWHRGVTKRSLSPHRPRHSRLQREPQVQWLEQQVAKRRTKRDVYQEPTDPKFPQQWYLSGVTQRDLNVKAAWAQGYTGHGIVVS
ILDDGIEKNHPDLAGNYDPGASFDVNDQDPDPQPRYTQMNDNRHGTRCAGEVAAVANNGVCGVGVAYNARIGGVRMLDGEVTDAVEARSLGLNPNHIHIYSASWGPEDDGKTVDGPARLAEEAFFRGVSQGRGGLGSIFVWASGNGGREH
DSCNCDGYTNSIYTLSISSATQFGNVPWYSEACSSTLATTYSSGNQNEKQIVTTDLRQKCTESHTGTSASAPLAAGIIALTLEANKNLTWRDMQHLVVQTSKPAHLNANDWATNGVGRKVSHSYGYGLLDAGAMVALAQNWTTVAPQRKC
IIDILTEPKDIGKRLEVRKTVTACLGEPNHITRLEHAQARLTLSYNRRGDLAIHLVSPMGTRSTLLAARPHDYSADGFNDWAFMTTHSWDEDPSGEWVLEIENTSEANNYGTLTKFTLVLYGTAPEGLPVPPESSGCKTLTSSQACVVCE
EGFSLHQKSCVQHCPPGFAPQVLDTHYSTENDVETIRASVCAPCHASCATCQGPALTDCLSCPSHASLDPVEQTCSRQSQSSRESPPQQQPPRLPPEVEAGQRLRAGLLPSHLPEVVAGLSCAFIVLVFVTVFLVLQLRSGFSFRGVKVY
TMDRGLISYKGLPPEAWQEECPSDSEEDEGRGERTAFIKDQSAL
[BLAST file for PDB] (plain) (bar) (multiple alignment) [BLAST for UniProt: (plain) (bar) (multiple alignment) (PSSM file) ]

UniProt Feature Tables [P09958(FURIN_HUMAN)]

794
region name description
1-26 SIGNAL
27-107 PROPEP /note="Inhibition peptide" /id="PRO_0000027028"
108-794 CHAIN /note="Furin" /id="PRO_0000027029"
108-715 TOPO_DOM /note="Lumenal"
716-738 TRANSMEM /note="Helical"
739-794 TOPO_DOM /note="Cytoplasmic"
121-435 DOMAIN /note="Peptidase S8"
444-576 DOMAIN /note="P/Homo B"
577-620 REPEAT /note="FU 1"
638-681 REPEAT /note="FU 2"
162-183 REGION /note="Disordered"
673-696 REGION /note="Disordered"
759-762 REGION /note="Cell surface signal"
767-794 REGION /note="Disordered"
673-687 COMPBIAS /note="Polar residues"
153-153 ACT_SITE /note="Charge relay system"
194-194 ACT_SITE /note="Charge relay system"
368-368 ACT_SITE /note="Charge relay system"
115-115 BINDING /ligand="Ca(2+)" /ligand_id="ChEBI:CHEBI:29108" /ligand_label="1" ECO:0000269|PubMed:25974265, ECO:0007744|PDB:4OMC, ECO:0007744|PDB:4OMD, ECO:0007744|PDB:4RYD"
154-154 BINDING /ligand="substrate" ECO:0000305|PubMed:25974265, ECO:0007744|PDB:4OMC, ECO:0007744|PDB:4OMD, ECO:0007744|PDB:4RYD"
162-162 BINDING /ligand="Ca(2+)" /ligand_id="ChEBI:CHEBI:29108" /ligand_label="1" ECO:0000269|PubMed:25974265, ECO:0007744|PDB:4OMC, ECO:0007744|PDB:4OMD, ECO:0007744|PDB:4RYD"
174-174 BINDING /ligand="Ca(2+)" /ligand_id="ChEBI:CHEBI:29108" /ligand_label="2" ECO:0000269|PubMed:25974265, ECO:0007744|PDB:4OMC, ECO:0007744|PDB:4OMD, ECO:0007744|PDB:4RYD"
179-179 BINDING /ligand="Ca(2+)" /ligand_id="ChEBI:CHEBI:29108" /ligand_label="2" ECO:0000269|PubMed:25974265, ECO:0007744|PDB:4OMC, ECO:0007744|PDB:4OMD, ECO:0007744|PDB:4RYD"
181-181 BINDING /ligand="Ca(2+)" /ligand_id="ChEBI:CHEBI:29108" /ligand_label="2" ECO:0000269|PubMed:25974265, ECO:0007744|PDB:4OMC, ECO:0007744|PDB:4OMD, ECO:0007744|PDB:4RYD"
191-192 BINDING /ligand="substrate" ECO:0000305|PubMed:25974265, ECO:0007744|PDB:4OMC, ECO:0007744|PDB:4OMD, ECO:0007744|PDB:4RYD"
205-205 BINDING /ligand="Ca(2+)" /ligand_id="ChEBI:CHEBI:29108" /ligand_label="1" ECO:0000269|PubMed:25974265, ECO:0007744|PDB:4OMC, ECO:0007744|PDB:4OMD, ECO:0007744|PDB:4RYD"
208-208 BINDING /ligand="Ca(2+)" /ligand_id="ChEBI:CHEBI:29108" /ligand_label="1" ECO:0000269|PubMed:25974265, ECO:0007744|PDB:4OMC, ECO:0007744|PDB:4OMD, ECO:0007744|PDB:4RYD"
210-210 BINDING /ligand="Ca(2+)" /ligand_id="ChEBI:CHEBI:29108" /ligand_label="1" ECO:0000269|PubMed:25974265, ECO:0007744|PDB:4OMC, ECO:0007744|PDB:4OMD, ECO:0007744|PDB:4RYD"
212-212 BINDING /ligand="Ca(2+)" /ligand_id="ChEBI:CHEBI:29108" /ligand_label="1" ECO:0000269|PubMed:25974265, ECO:0007744|PDB:4OMC, ECO:0007744|PDB:4OMD, ECO:0007744|PDB:4RYD"
236-236 BINDING /ligand="substrate" ECO:0000305|PubMed:25974265, ECO:0007744|PDB:4OMC, ECO:0007744|PDB:4OMD, ECO:0007744|PDB:4RYD"
253-258 BINDING /ligand="substrate" ECO:0000305|PubMed:25974265, ECO:0007744|PDB:4OMC, ECO:0007744|PDB:4OMD, ECO:0007744|PDB:4RYD"
258-258 BINDING /ligand="Ca(2+)" /ligand_id="ChEBI:CHEBI:29108" /ligand_label="3" ECO:0000269|PubMed:25974265, ECO:0007744|PDB:4OMC, ECO:0007744|PDB:4OMD, ECO:0007744|PDB:4RYD"
264-264 BINDING /ligand="substrate" ECO:0000305|PubMed:25974265, ECO:0007744|PDB:4OMC, ECO:0007744|PDB:4OMD, ECO:0007744|PDB:4RYD"
292-295 BINDING /ligand="substrate" ECO:0000305|PubMed:25974265, ECO:0007744|PDB:4OMC, ECO:0007744|PDB:4OMD, ECO:0007744|PDB:4RYD"
301-301 BINDING /ligand="Ca(2+)" /ligand_id="ChEBI:CHEBI:29108" /ligand_label="3" ECO:0000269|PubMed:25974265, ECO:0007744|PDB:4OMC, ECO:0007744|PDB:4OMD, ECO:0007744|PDB:4RYD"
306-306 BINDING /ligand="substrate" ECO:0000305|PubMed:25974265, ECO:0007744|PDB:4OMC, ECO:0007744|PDB:4OMD, ECO:0007744|PDB:4RYD"
308-308 BINDING /ligand="substrate" ECO:0000305|PubMed:25974265, ECO:0007744|PDB:4OMC, ECO:0007744|PDB:4OMD, ECO:0007744|PDB:4RYD"
331-331 BINDING /ligand="Ca(2+)" /ligand_id="ChEBI:CHEBI:29108" /ligand_label="3" ECO:0000269|PubMed:25974265, ECO:0007744|PDB:4OMC, ECO:0007744|PDB:4OMD, ECO:0007744|PDB:4RYD"
368-368 BINDING /ligand="substrate" ECO:0000305|PubMed:25974265, ECO:0007744|PDB:4OMC, ECO:0007744|PDB:4OMD, ECO:0007744|PDB:4RYD"
1-794 DISORDER predicted by DISOPRED

MONOMER
794
pdb_id a1 identity[%]2 description
5jmo B 99.4 FURIN_HUMAN Furin
6a8y A 100.0 FURIN_HUMAN YR26_SDS
3whi B 35.7 SUBT_BACSU Subtilisin E
1kn6 A 38.6 NEC1_MOUSE Prohormone Convertase 1 
1.a1:asym_id for the homologue. 2.identity[%]2:sequence identity between the query and the homologue.
HETERO
794 pdb_id contact mol homologue
a3 description a4 identity[%]5 Ncon6 description
6hlb[1] B PHE-(ALN)-ARG-ARG-ARG-ARG-SLL-ARG-00S[7 aa] A 100.0
/100.0		 27
/27		 FURIN_HUMAN Furin
1p8j[11] I DECANOYL-ARG-VAL-LYS-ARG-CHLOROMETHYLKETONE INHIBI.. A 100.0
/97.9		 25
/25		 FURI_MOUSE Furin precursor
1p8j[4] K DECANOYL-ARG-VAL-LYS-ARG-CHLOROMETHYLKETONE INHIBI.. B 100.0
/97.9		 4
/4		 FURI_MOUSE Furin precursor
5jmo[2] C camelid VHH fragment[115 aa] A 100.0
/99.4		 15
/15		 FURIN_HUMAN Furin
4omc[14] G meta-guanidinomethyl-phenylacetyl-Arg-Val-Arg-(ami.. A 100.0
/100.0		 27
/27		 FURIN_HUMAN Furin
4ryd[7] G para-guanidinomethyl-phenylacetyl-Arg-(3-methylval.. A 100.0
/100.0		 28
/28		 FURIN_HUMAN Furin
6eqv[1] B HY1-LLI-VAL-ARG-00S[5 aa] A 100.0
/99.4		 25
/25		 FURIN_HUMAN Furin
6eqx[1] B Arg-Arg-Arg-Val-Arg-00S[6 aa] A 100.0
/99.4		 28
/28		 FURIN_HUMAN Furin
6hld[1] B ALN-ARG-ARG-ARG-SLL-LYS-00S[7 aa] A 100.0
/99.4		 27
/27		 FURIN_HUMAN Furin
6hle[2] B LYS-ARG-ARG-TBG-LYS-00S[6 aa] A 100.0
/99.4		 26
/26		 FURIN_HUMAN Furin
6hza[1] B ARG-ARG-LYS-ARG-00S[5 aa] A 100.0
/99.4		 27
/27		 FURIN_HUMAN Furin
6hzb[1] B ARG-ARG-LYS-LYS-00S[5 aa] A 100.0
/99.4		 28
/28		 FURIN_HUMAN Furin
6hzd[1] B ARG-ARG-ARG-LYS-ARG-00S[6 aa] A 100.0
/99.4		 28
/28		 FURIN_HUMAN Furin
6yd2[2] B 4-aminomethyl-phenylacetyl-canavanine-Tle-Arg-Amba.. A 100.0
/99.4		 25
/25		 FURIN_HUMAN Furin
6yd4[2] B 4-guanidinomethyl-phenylacetyl-Canavanine-Tle-Cana.. A 100.0
/99.4		 28
/28		 FURIN_HUMAN Furin
6yd7[1] B 4-guanidinomethyl-phenylacetyl-Arg-Tle-Canavanine-.. A 100.0
/99.4		 28
/28		 FURIN_HUMAN Furin
8b4x[1] B Guanidinomethyl-Phac-R-Tle-K-6-(aminomethyl)-3-ami.. A 100.0
/99.4		 28
/28		 FURIN_HUMAN Furin
1oyv[2] C IP21_LYCES Wound-induced proteinase inhibitor-II[104 aa] A 50.0
/49.2		 2
/27		 SUBT_BACLI Subtilisin Carlsberg
1r0r[3] B IOVO_MELGA Ovomucoid[51 aa] A 50.0
/49.2		 2
/23		 SUBT_BACLI subtilisin carlsberg
3qtl[2] D A1X1V8_CARRO Kazal-type serine protease inhibitor SPI-1[75 aa] A 100.0
/49.2		 1
/21		 Q1EM64_BACLI Subtilisin-like serin protease
4gi3[1] B SPI_SCHGR Greglin[57 aa] A 100.0
/49.2		 1
/21		 Q9FDF2_BACLI KerA
4hx2[2] B Q9FDS0_STRCS Neutral proteinase inhibitor ScNPI[114 aa] A 100.0
/49.2		 1
/21		 Q9FDF2_BACLI KerA
5ox2[1] B Fragment of prodomain[9 aa] A 100.0
/48.6		 1
/15		 SUBT_BACAM Subtilisin BPN'
1sua[1] B TETRAPEPTIDE ALA-LEU-ALA-LEU[4 aa] A 100.0
/47.1		 1
/16		 SUBT_BACAM SUBTILISIN BPN'
3bgo[3] A SUBT_BACAM Subtilisin BPN' [71 aa] B 100.0
/47.1		 1
/38		 SUBT_BACAM Subtilisin BPN'
6ube[1] B Peptide LFRAL[5 aa] A 100.0
/47.1		 1
/22		 SUBTILISIN BPN'
8coy[2] C peptido-mimetic inhibitor[7 aa] A 66.7
/45.8		 3
/19		 E6Y8B9_PLAVI subtilisin
8qke[6] C Peptidomimetic Inhibitor (MH-13)[7 aa] A 66.7
/45.8		 3
/20		 E6Y8B9_PLAVI subtilisin
1spb[1] A SUBT_BACAM SUBTILISIN BPN' PROSEGMENT [71 aa] B 100.0
/45.7		 1
/34		 SUBT_BACAM SUBTILISIN BPN'
1cse[5] B ICIC_HIRME EGLIN C[63 aa] A 66.7
/49.2		 3
/26		 SUBT_BACLI SUBTILISIN CARLSBERG
1tec[3] B ICIC_HIRME EGLIN C[63 aa] A 75.0
/44.7		 4
/27		 THET_THEVU THERMITASE
8h7p[1] B 5,6-DIHYDRO-BENZO[H]CINNOLIN-3-YLAMINE[6 aa] A 100.0
/42.4		 2
/19		 A0A7U5AV24_BACIU Subtilisin
2id4[2] C Ac-RERK-CMK inhibitor[6 aa] A 68.4
/42.3		 19
/19		 KEX2_YEAST Kexin
1ot5[2] C Ac-Ala-Lys-boroArg N-acetylated boronic acid pepti.. A 94.7
/42.2		 19
/19		 KEX2_YEAST Kexin
1r64[2] C Ac-Arg-Glu-Lys-boroArg peptide inhibitor[5 aa] A 83.3
/42.2		 24
/24		 KEX2_YEAST Kexin
1lw6[32] B ICI2_HORVU SUBTILISIN-CHYMOTRYPSIN INHIBITOR-2A[63 aa] A 66.7
/40.9		 3
/24		 SUBT_BACAM SUBTILISIN BPN'
1v5i[1] B PIA1_PLEOS IA-1=serine proteinase inhibitor[76 aa] A 100.0
/40.9		 2
/26		 SUBT_BACAM Subtilisin BPN'
2sic[6] B SSI_STRAO STREPTOMYCES SUBTILISIN INHIBITOR (SSI)[107 aa] A 50.0
/40.9		 2
/23		 SUBT_BACAM SUBTILISIN BPN'
1scj[1] B SUBT_BACSU SUBTILISIN E[71 aa] A 50.0
/40.7		 2
/32		 SUBT_BACSU SUBTILISIN E
1tk2[1] B GRAMICIDIN S[10 aa] A 38.5
/37.0		 13
/13		 SUBS_BACLE SUBTILISIN SAVINASE
3bx1[4] C IAAS_HORVU Alpha-amylase/subtilisin inhibitor[181 aa] A 38.5
/37.0		 13
/16		 SUBS_BACLE Subtilisin Savinase
3bx1[4] D IAAS_HORVU Alpha-amylase/subtilisin inhibitor[181 aa] A 39.3
/37.0		 28
/28		 SUBS_BACLE Subtilisin Savinase
3bx1[2] D IAAS_HORVU Alpha-amylase/subtilisin inhibitor[181 aa] A 25.0
/37.0		 8
/10		 SUBS_BACLE Subtilisin Savinase
8ehe[1] B A0A1D3UUC0_TANFO Potempin C (PotC)[124 aa] A 46.9
/33.6		 32
/34		 A0A0A7KVG3_TANFO Mirolase
5yl7[1] B Copurified unknown peptide[3 aa] A 55.6
/31.1		 9
/9		 Pseudoalteromonas arctica PAMC 21717
3wqb[1] B Open reading frame 2[99 aa] A 33.3
/31.0		 27
/35		 Q9L5A4_AERSO Extracellular serine protease
2b6n[1] B TRIPEPTIDE[3 aa] A 50.0
/29.7		 8
/8		 Q3HUQ2_9ENTR proteinase K
4lvn[2] B NIMP.M7 Fab light chain[207 aa] A 0.0
/26.9		 2
/7		 Q868D6_PLAFA Subtilisin-like serine protease
4lvn[2] D Q868D6_PLAFA Subtilisin-like serine protease[81 aa] A 23.1
/26.9		 26
/28		 Q868D6_PLAFA Subtilisin-like serine protease
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
794 pdb_id contact mol homologue
a3 description a4 identity[%]5 Ncon6 description
7o1w[2] B UYQ
[[(2E)-2-[[4-[(E)-[[azaniumylidene(azanyl)methyl]h.. 		A 100.0
/99.4		 11
/11		 FURIN_HUMAN Furin
7o1w[2] C UYQ
[[(2E)-2-[[4-[(E)-[[azaniumylidene(azanyl)methyl]h.. 		A 100.0
/99.4		 8
/8		 FURIN_HUMAN Furin
7o1w[2] D UYQ
[[(2E)-2-[[4-[(E)-[[azaniumylidene(azanyl)methyl]h.. 		A 100.0
/99.4		 5
/5		 FURIN_HUMAN Furin
7o20[1] B UYT
[azanyl-[(2E)-2-(1-phenylethylidene)hydrazinyl]met.. 		A 100.0
/100.0		 7
/7		 FURIN_HUMAN Furin
7o20[1] C UYT
[azanyl-[(2E)-2-(1-phenylethylidene)hydrazinyl]met.. 		A 100.0
/100.0		 8
/8		 FURIN_HUMAN Furin
7o20[1] D UYT
[azanyl-[(2E)-2-(1-phenylethylidene)hydrazinyl]met.. 		A 100.0
/100.0		 5
/5		 FURIN_HUMAN Furin
7o22[1] M UYW
[azanyl-[(2E)-2-[[2-[(4-chlorophenyl)methoxy]pheny.. 		A 100.0
/100.0		 14
/14		 FURIN_HUMAN Furin
5mim[1] J 1N
1-[(1~{R},2~{R},4~{S},5~{S})-2,4-bis(4-carbamimida.. 		A 100.0
/99.4		 7
/7		 FURIN_HUMAN Furin
5mim[1] K 1N
1-[(1~{R},2~{R},4~{S},5~{S})-2,4-bis(4-carbamimida.. 		A 100.0
/99.4		 14
/14		 FURIN_HUMAN Furin
6hle[1] M GEB
3-[4-(3-oxidanylidenepropyl)piperazin-1-yl]propana.. 		A 100.0
/99.4		 4
/4		 FURIN_HUMAN Furin
6hza[3] M PTD
PENTANEDIAL[7 atoms] 		A 100.0
/99.4		 1
/1		 FURIN_HUMAN Furin
6hzc[1] M PTD
PENTANEDIAL[7 atoms] 		A 100.0
/99.4		 5
/5		 FURIN_HUMAN Furin
6hzc[1] N BVK
2-[4-(aminomethyl)phenyl]ethanoic acid[11 atoms] 		A 100.0
/99.4		 1
/1		 FURIN_HUMAN Furin
7qxy[1] J I1G
3-[4-[5-[4-[[4-(acetamidomethyl)piperidin-1-ium-1-.. 		A 100.0
/99.4		 18
/18		 FURIN_HUMAN Furin
7qxz[1] H I0M
2-[(3S)-1-[[2-[3,5-bis(chloranyl)phenyl]-6-[2-(4-m.. 		A 100.0
/99.4		 16
/16		 FURIN_HUMAN Furin
1ot5[24] G NAG
2-acetamido-2-deoxy-beta-D-glucopyranose[14 atoms].. 		A 33.3
/42.2		 3
/3		 KEX2_YEAST Kexin
1r64[1] H NAG
2-acetamido-2-deoxy-beta-D-glucopyranose[14 atoms].. 		A 57.1
/42.2		 7
/7		 KEX2_YEAST Kexin
2id4[2] G NAG
2-acetamido-2-deoxy-beta-D-glucopyranose[14 atoms].. 		A 0.0
/42.3		 1
/1		 KEX2_YEAST Kexin
7o1u[1] B UYN
[[(2E)-2-[1-[3-[(E)-N-[[azaniumylidene(azanyl)meth.. 		A 100.0
/99.4		 9
/9		 FURIN_HUMAN Furin
7qy0[1] B I0T
N-[[1-[[2-[3,5-bis(chloranyl)phenyl]-6-[6-[4-(2-me.. 		A 100.0
/99.4		 17
/17		 FURIN_HUMAN Furin
7qy1[1] B I0W
3-[4-[5-[4-[[4-(acetamidomethyl)piperidin-1-ium-1-.. 		A 100.0
/99.4		 17
/17		 FURIN_HUMAN Furin
7qy2[1] B I0Q
(2R)-4-[4-[5-[4-[[4-(acetamidomethyl)piperidin-1-i.. 		A 100.0
/99.4		 17
/17		 FURIN_HUMAN Furin
8b4v[1] B BEN
BENZAMIDINE[9 atoms] 		A 100.0
/99.4		 11
/11		 FURIN_HUMAN Furin
8b4v[1] C BEN
BENZAMIDINE[9 atoms] 		A 100.0
/99.4		 2
/2		 FURIN_HUMAN Furin
8b4w[1] B F05
1H-isoindol-3-amine[10 atoms] 		A 100.0
/99.4		 12
/12		 FURIN_HUMAN Furin
8b4w[1] C F05
1H-isoindol-3-amine[10 atoms] 		A 100.0
/99.4		 7
/7		 FURIN_HUMAN Furin
8b4w[1] D F05
1H-isoindol-3-amine[10 atoms] 		A 100.0
/99.4		 1
/1		 FURIN_HUMAN Furin
7lcu[1] F XTA
(1-{[2-(3,5-dichlorophenyl)-6-{[2-(4-methylpiperaz.. 		A 100.0
/99.1		 16
/16		 FURIN_HUMAN Furin
1be6[2] C TCA
PHENYLETHYLENECARBOXYLIC ACID[10 atoms] 		A 100.0
/49.2		 1
/8		 SUBT_BACLI SUBTILISIN CARLSBERG
1scn[1] B 0EF
N-(tert-butoxycarbonyl)-L-alanyl-N-[(1R)-1-(carbox.. 		A 100.0
/49.2		 1
/11		 SUBT_BACLI SUBTILISIN CARLSBERG
4hx2[1] I 1AX
(2R,2'R)-3,3'-oxydipropane-1,2-diol[11 atoms] 		A 0.0
/49.2		 2
/8		 Q9FDF2_BACLI KerA
1dui[2] C DFP
DIISOPROPYL PHOSPHONATE[7 atoms] 		A 100.0
/47.1		 1
/8		 SUBT_BACAM PROTEIN (SUBTILISIN BPN')
7am6[1] F TAR
D(-)-TARTARIC ACID[10 atoms] 		B 100.0
/47.1		 1
/8		 SUBT_BACAM Subtilisin BPN'
7am6[1] L TAR
D(-)-TARTARIC ACID[10 atoms] 		C 0.0
/47.1		 6
/7		 SUBT_BACAM Subtilisin BPN'
2id4[1] K MLA
MALONIC ACID[7 atoms] 		A 75.0
/42.3		 4
/4		 KEX2_YEAST Kexin
1r64[1] V BTB
2-[BIS-(2-HYDROXY-ETHYL)-AMINO]-2-HYDROXYMETHYL-PR.. 		B 0.0
/42.2		 5
/5		 KEX2_YEAST Kexin
1s2n[4] F PMS
phenylmethanesulfonic acid[10 atoms] 		A 57.1
/30.2		 7
/10		 Q8GB52_9VIBR extracellular subtilisin-like serine proteinase
1sup[1] D PMS
phenylmethanesulfonic acid[10 atoms] 		A 100.0
/40.9		 1
/9		 SUBT_BACAM SUBTILISIN BPN'
1tmg[16] J 15P
POLYETHYLENE GLYCOL (N=34)[19 atoms] 		A 14.3
/40.9		 7
/7		 SUBT_BACAM Subtilisin BPN'
1to2[15] G 15P
POLYETHYLENE GLYCOL (N=34)[8 atoms] 		A 66.7
/40.9		 3
/3		 SUBT_BACAM Subtilisin BPN'
1y34[4] K 15P
POLYETHYLENE GLYCOL (N=34)[11 atoms] 		A 100.0
/40.9		 2
/4		 SUBT_BACAM subtilisin BPN'
1y3d[2] K 15P
POLYETHYLENE GLYCOL (N=34)[17 atoms] 		A 0.0
/40.9		 1
/2		 SUBT_BACAM subtilisin BPN'
5aqe[1] B VOD
(4-VINYLPHENYL)METHANESULFONIC ACID[12 atoms] 		A 84.6
/37.0		 13
/13		 SUBS_BACLE SUBTILISIN SAVINASE
5arb[2] F EI3
5-methyl-2-(5-methylpyridin-2-yl)pyridine[14 atoms.. 		A 33.3
/37.0		 3
/4		 SUBS_BACLE SUBTILISIN SAVINASE
5arc[1] C EI3
5-methyl-2-(5-methylpyridin-2-yl)pyridine[14 atoms.. 		A 25.0
/37.0		 4
/4		 SUBS_BACLE SUBTILISIN SAVINASE
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
794 pdb_id contact mol homologue
a3 description a4 identity[%]5 Ncon6 description
1av7[3] C NA
SODIUM ION[1 atoms] 		A 60.0
/49.2		 5
/6		 SUBT_BACLI SUBTILISIN CARLSBERG, TYPE VIII
2id4[2] J NA
SODIUM ION[1 atoms] 		A 60.0
/42.3		 5
/5		 KEX2_YEAST Kexin
2wuw[5] C NA
SODIUM ION[1 atoms] 		A 50.0
/49.2		 4
/4		 SUBT_BACLI SUBTILISIN CARLSBERG
3bx1[2] Q NA
SODIUM ION[1 atoms] 		A 0.0
/37.0		 2
/2		 SUBS_BACLE Subtilisin Savinase
3bx1[4] R NA
SODIUM ION[1 atoms] 		A 50.0
/37.0		 2
/2		 SUBS_BACLE Subtilisin Savinase
3bx1[9] S NA
SODIUM ION[1 atoms] 		A 33.3
/37.0		 6
/6		 SUBS_BACLE Subtilisin Savinase
4omc[53] T NA
SODIUM ION[1 atoms] 		A 100.0
/100.0		 5
/5		 FURIN_HUMAN Furin
5jxg[9] F NA
SODIUM ION[1 atoms] 		A 100.0
/99.4		 2
/2		 FURIN_HUMAN Furin
5jxg[22] H NA
SODIUM ION[1 atoms] 		A 100.0
/99.4		 2
/2		 FURIN_HUMAN Furin
5jxg[29] I NA
SODIUM ION[1 atoms] 		A 100.0
/99.4		 2
/2		 FURIN_HUMAN Furin
5jxg[7] J NA
SODIUM ION[1 atoms] 		A 100.0
/99.4		 1
/1		 FURIN_HUMAN Furin
5jxg[11] L NA
SODIUM ION[1 atoms] 		A 100.0
/99.4		 1
/1		 FURIN_HUMAN Furin
5jxi[2] G NA
SODIUM ION[1 atoms] 		A 100.0
/99.4		 3
/3		 FURIN_HUMAN Furin
5jxi[2] H NA
SODIUM ION[1 atoms] 		A 100.0
/99.4		 4
/4		 FURIN_HUMAN Furin
6f9m[2] D NA
SODIUM ION[1 atoms] 		A 20.0
/38.2		 5
/5		 Serine protease
6uai[1] D NA
SODIUM ION[1 atoms] 		A 0.0
/50.7		 1
/2		 SUBTILISIN BPN'
7qy0[3] I NA
SODIUM ION[1 atoms] 		A 100.0
/99.4		 4
/4		 FURIN_HUMAN Furin
2wuv[1] H CL
CHLORIDE ION[1 atoms] 		A 66.7
/49.2		 3
/3		 SUBT_BACLI SUBTILISIN CARLSBERG
3bx1[2] F CL
CHLORIDE ION[1 atoms] 		A 50.0
/37.0		 2
/3		 SUBS_BACLE Subtilisin Savinase
3bx1[4] G CL
CHLORIDE ION[1 atoms] 		A 25.0
/37.0		 4
/4		 SUBS_BACLE Subtilisin Savinase
3bx1[2] H CL
CHLORIDE ION[1 atoms] 		A 100.0
/37.0		 2
/2		 SUBS_BACLE Subtilisin Savinase
3bx1[2] IA CL
CHLORIDE ION[1 atoms] 		A 0.0
/37.0		 1
/1		 SUBS_BACLE Subtilisin Savinase
3bx1[2] J CL
CHLORIDE ION[1 atoms] 		A 0.0
/37.0		 2
/2		 SUBS_BACLE Subtilisin Savinase
3bx1[2] K CL
CHLORIDE ION[1 atoms] 		A 0.0
/37.0		 1
/1		 SUBS_BACLE Subtilisin Savinase
3bx1[4] L CL
CHLORIDE ION[1 atoms] 		A 33.3
/37.0		 3
/3		 SUBS_BACLE Subtilisin Savinase
3bx1[2] M CL
CHLORIDE ION[1 atoms] 		A 16.7
/37.0		 6
/6		 SUBS_BACLE Subtilisin Savinase
3bx1[6] N CL
CHLORIDE ION[1 atoms] 		A 33.3
/37.0		 3
/4		 SUBS_BACLE Subtilisin Savinase
3bx1[2] O CL
CHLORIDE ION[1 atoms] 		A 0.0
/37.0		 1
/1		 SUBS_BACLE Subtilisin Savinase
3bx1[3] X CL
CHLORIDE ION[1 atoms] 		B 100.0
/37.0		 1
/3		 SUBS_BACLE Subtilisin Savinase
3bx1[2] Z CL
CHLORIDE ION[1 atoms] 		B 100.0
/37.0		 4
/4		 SUBS_BACLE Subtilisin Savinase
3ti9[1] F CL
CHLORIDE ION[1 atoms] 		A 0.0
/35.7		 1
/3		 Q46547_DICNO Serine protease
4hx2[1] H CL
CHLORIDE ION[1 atoms] 		A 100.0
/49.2		 1
/2		 Q9FDF2_BACLI KerA
5jxg[33] M CL
CHLORIDE ION[1 atoms] 		A 100.0
/99.4		 3
/3		 FURIN_HUMAN Furin
1r64[2] L K
POTASSIUM ION[1 atoms] 		A 33.3
/42.2		 3
/4		 KEX2_YEAST Kexin
1r64[2] M K
POTASSIUM ION[1 atoms] 		A 0.0
/42.2		 3
/3		 KEX2_YEAST Kexin
1r64[1] N K
POTASSIUM ION[1 atoms] 		A 100.0
/42.2		 1
/1		 KEX2_YEAST Kexin
1r64[1] U K
POTASSIUM ION[1 atoms] 		B 0.0
/42.2		 1
/1		 KEX2_YEAST Kexin
6u9l[1] D K
POTASSIUM ION[1 atoms] 		A 50.0
/50.7		 4
/4		 SUBTILISIN BPN'
2wuv[2] I CS
CESIUM ION[1 atoms] 		A 50.0
/49.2		 4
/4		 SUBT_BACLI SUBTILISIN CARLSBERG
2wuv[2] K CS
CESIUM ION[1 atoms] 		A 0.0
/49.2		 1
/2		 SUBT_BACLI SUBTILISIN CARLSBERG
2wuv[2] Q CS
CESIUM ION[1 atoms] 		A 100.0
/49.2		 1
/3		 SUBT_BACLI SUBTILISIN CARLSBERG
4c3u[1] M CS
CESIUM ION[1 atoms] 		A 50.0
/49.2		 2
/2		 SUBT_BACLI SUBTILISIN CARLSBERG
3bgo[3] F ZN
ZINC ION[1 atoms] 		B 100.0
/47.1		 3
/3		 SUBT_BACAM Subtilisin BPN'
3bgo[3] G ZN
ZINC ION[1 atoms] 		B 0.0
/47.1		 1
/1		 SUBT_BACAM Subtilisin BPN'
1a2q[199] B CA
CALCIUM ION[1 atoms] 		A 40.0
/39.8		 5
/6		 SUBT_BACAM SUBTILISIN BPN'
1c9j[13] D CA
CALCIUM ION[1 atoms] 		A 28.6
/37.0		 7
/7		 SUBS_BACLE SERINE PROTEASE
1dbi[1] B CA
CALCIUM ION[1 atoms] 		A 40.0
/45.1		 5
/6		 THES_BACSJ AK.1 SERINE PROTEASE
1dbi[1] E CA
CALCIUM ION[1 atoms] 		A 33.3
/45.1		 3
/3		 THES_BACSJ AK.1 SERINE PROTEASE
1ot5[2] H CA
CALCIUM ION[1 atoms] 		A 100.0
/42.2		 3
/3		 KEX2_YEAST Kexin
1ot5[4] I CA
CALCIUM ION[1 atoms] 		A 66.7
/42.2		 6
/6		 KEX2_YEAST Kexin
1ot5[4] J CA
CALCIUM ION[1 atoms] 		A 40.0
/42.2		 5
/5		 KEX2_YEAST Kexin
1p8j[64] T CA
CALCIUM ION[1 atoms] 		A 100.0
/97.9		 6
/6		 FURI_MOUSE Furin precursor
1p8j[61] U CA
CALCIUM ION[1 atoms] 		A 100.0
/97.9		 3
/3		 FURI_MOUSE Furin precursor
1r0r[4] C CA
CALCIUM ION[1 atoms] 		A 50.0
/49.2		 4
/4		 SUBT_BACLI subtilisin carlsberg
1r64[2] I CA
CALCIUM ION[1 atoms] 		A 100.0
/42.2		 3
/3		 KEX2_YEAST Kexin
1s2n[4] E CA
CALCIUM ION[1 atoms] 		A 20.0
/30.2		 5
/5		 Q8GB52_9VIBR extracellular subtilisin-like serine proteinase
1tec[4] C CA
CALCIUM ION[1 atoms] 		A 66.7
/44.7		 6
/6		 THET_THEVU THERMITASE
1tec[6] D CA
CALCIUM ION[1 atoms] 		A 80.0
/44.7		 5
/5		 THET_THEVU THERMITASE
2b6n[1] C CA
CALCIUM ION[1 atoms] 		A 20.0
/29.7		 5
/5		 Q3HUQ2_9ENTR proteinase K
2id4[2] H CA
CALCIUM ION[1 atoms] 		A 100.0
/42.3		 3
/3		 KEX2_YEAST Kexin
2id4[10] I CA
CALCIUM ION[1 atoms] 		A 66.7
/42.3		 6
/6		 KEX2_YEAST Kexin
3hjr[4] B CA
CALCIUM ION[1 atoms] 		A 50.0
/31.3		 6
/6		 Q9L5A4_AERSO Extracellular serine protease
3hjr[2] C CA
CALCIUM ION[1 atoms] 		A 50.0
/31.3		 4
/6		 Q9L5A4_AERSO Extracellular serine protease
3hjr[2] D CA
CALCIUM ION[1 atoms] 		A 66.7
/31.3		 3
/6		 Q9L5A4_AERSO Extracellular serine protease
3lpa[3] C CA
CALCIUM ION[1 atoms] 		A 66.7
/32.6		 6
/6		 A5EXI3_DICNV Acidic extracellular subtilisin-like protease AprV..
3whi[3] C CA
CALCIUM ION[1 atoms] 		A 50.0
/36.6		 6
/6		 SUBT_BACSU Subtilisin E
4lvn[2] F CA
CALCIUM ION[1 atoms] 		A 40.0
/26.9		 5
/6		 Q868D6_PLAFA Subtilisin-like serine protease
4tr2[4] C CA
CALCIUM ION[1 atoms] 		A 60.0
/45.8		 5
/6		 E6Y8B9_PLAVI Subtilisin-like 1 serine protease
4z2a[2] D CA
CALCIUM ION[1 atoms] 		A 100.0
/99.6		 4
/4		 FURIN_HUMAN Furin
4z2a[1] E CA
CALCIUM ION[1 atoms] 		A 100.0
/99.6		 3
/3		 FURIN_HUMAN Furin
5yl7[1] F CA
CALCIUM ION[1 atoms] 		A 0.0
/31.1		 3
/3		 Pseudoalteromonas arctica PAMC 21717
8cp0[1] B CA
CALCIUM ION[1 atoms] 		A 60.0
/45.8		 5
/6		 E6Y8B9_PLAVI subtilisin
8e7f[1] M CA
CALCIUM ION[1 atoms] 		A 0.0
/38.1		 6
/6		 PRTS_SERMA Extracellular serine protease
8ehe[1] D CA
CALCIUM ION[1 atoms] 		A 25.0
/33.6		 4
/4		 A0A0A7KVG3_TANFO Mirolase
8ehe[1] E CA
CALCIUM ION[1 atoms] 		A 33.3
/33.6		 3
/6		 A0A0A7KVG3_TANFO Mirolase
8ehe[1] F CA
CALCIUM ION[1 atoms] 		A 40.0
/33.6		 5
/5		 A0A0A7KVG3_TANFO Mirolase
8ehe[1] H CA
CALCIUM ION[1 atoms] 		A 66.7
/33.6		 3
/3		 A0A0A7KVG3_TANFO Mirolase
8ehe[1] I CA
CALCIUM ION[1 atoms] 		A 50.0
/33.6		 4
/4		 A0A0A7KVG3_TANFO Mirolase
8pol[2] D CA
CALCIUM ION[1 atoms] 		A 0.0
/27.4		 2
/5		 SUB1_PLAF7 Subtilisin-like protease 1
8pol[2] F CA
CALCIUM ION[1 atoms] 		A 33.3
/27.4		 6
/7		 SUB1_PLAF7 Subtilisin-like protease 1
8qke[6] E CA
CALCIUM ION[1 atoms] 		A 60.0
/45.8		 5
/6		 E6Y8B9_PLAVI subtilisin
8e7f[1] J IOD
IODIDE ION[1 atoms] 		A 100.0
/38.1		 1
/2		 PRTS_SERMA Extracellular serine protease
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
794 pdb_id contact mol homologue
a3 description a4 identity[%]5 Ncon6 description
1p8j[1] Q beta-D-galactopyranose-(1-4)-2-acetamido-2-deoxy-b.. A 100.0
/97.9		 1
/1		 FURI_MOUSE Furin precursor
1p8j[1] Q beta-D-galactopyranose-(1-4)-2-acetamido-2-deoxy-b.. G 91.7
/97.9		 12
/12		 FURI_MOUSE Furin precursor
1p8j[1] R beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-bet.. A 100.0
/97.9		 1
/1		 FURI_MOUSE Furin precursor
1p8j[2] R beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-bet.. G 100.0
/97.9		 3
/3		 FURI_MOUSE Furin precursor
2id4[2] E 2-acetamido-2-deoxy-alpha-D-glucopyranose-(1-4)-2-.. A 0.0
/42.3		 3
/3		 KEX2_YEAST Kexin
1ot5[2] E 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-a.. A 0.0
/42.2		 4
/4		 KEX2_YEAST Kexin
1r64[2] E 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-a.. A 0.0
/42.2		 4
/4		 KEX2_YEAST Kexin
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
794 pdb_id contact mol homologue
a3 description a4 identity[%]5 Ncon6 description
1p8j[8] B FURI_MOUSE Furin precursor[468 aa] A 92.0
/97.9		 25
/25		 FURI_MOUSE Furin precursor
1p8j[12] C FURI_MOUSE Furin precursor[467 aa] A 100.0
/97.9		 5
/5		 FURI_MOUSE Furin precursor
1p8j[4] D FURI_MOUSE Furin precursor[467 aa] A 100.0
/97.9		 6
/6		 FURI_MOUSE Furin precursor
1p8j[1] G FURI_MOUSE Furin precursor[467 aa] A 100.0
/97.9		 11
/11		 FURI_MOUSE Furin precursor
1p8j[1] A FURI_MOUSE Furin precursor[470 aa] G 90.9
/97.9		 11
/11		 FURI_MOUSE Furin precursor
3qtl[1] A Q1EM64_BACLI Subtilisin-like serin protease[269 aa] B 0.0
/49.2		 2
/2		 Q1EM64_BACLI Subtilisin-like serin protease
3qtl[1] A Q1EM64_BACLI Subtilisin-like serin protease[269 aa] C 0.0
/49.2		 3
/7		 Q1EM64_BACLI Subtilisin-like serin protease
8jmw[14] L A0A6A8LCF5_9BACI S8 family serine peptidase[517 aa] A 28.6
/48.2		 7
/10		 A0A6A8LCF5_9BACI S8 family serine peptidase
4tr2[1] B E6Y8B9_PLAVI Subtilisin-like 1 serine protease[474 aa] A 50.0
/45.8		 2
/42		 E6Y8B9_PLAVI Subtilisin-like 1 serine protease
4tr2[1] A E6Y8B9_PLAVI Subtilisin-like 1 serine protease[471 aa] B 50.0
/45.8		 2
/39		 E6Y8B9_PLAVI Subtilisin-like 1 serine protease
7y6m[2] C Intracellular serine protease[7 aa] A 100.0
/41.4		 3
/20		 Intracellular serine protease
1tm1[16] A SUBT_BACAM Subtilisin BPN' precursor [281 aa] A 100.0
/40.9		 1
/6		 SUBT_BACAM Subtilisin BPN' precursor
1tm3[8] A SUBT_BACAM Subtilisin BPN' precursor [281 aa] A 66.7
/40.9		 6
/9		 SUBT_BACAM Subtilisin BPN' precursor
3bx1[2] A SUBS_BACLE Subtilisin Savinase[269 aa] A 27.3
/37.0		 11
/11		 SUBS_BACLE Subtilisin Savinase
3whi[2] A SUBT_BACSU Subtilisin E[355 aa] A 14.3
/36.6		 7
/12		 SUBT_BACSU Subtilisin E
8pol[1] B SUB1_PLAF7 Subtilisin-like protease 1[479 aa] A 25.0
/27.4		 4
/32		 SUB1_PLAF7 Subtilisin-like protease 1
8pol[1] A SUB1_PLAF7 Subtilisin-like protease 1[477 aa] B 0.0
/27.4		 4
/29		 SUB1_PLAF7 Subtilisin-like protease 1
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
794 pdb_id contact mol homologue
a3 description a4 identity[%]5 Ncon6 description
1c3l[1] E FMT
FORMIC ACID[3 atoms] 		A 100.0
/49.2		 1
/6		 SUBT_BACLI SUBTILISIN-CARLSBERG
1c3l[1] G FMT
FORMIC ACID[3 atoms] 		A 100.0
/49.2		 1
/3		 SUBT_BACLI SUBTILISIN-CARLSBERG
4omc[12] M FMT
FORMIC ACID[3 atoms] 		A 100.0
/100.0		 4
/4		 FURIN_HUMAN Furin
4omc[6] N FMT
FORMIC ACID[3 atoms] 		A 100.0
/100.0		 5
/5		 FURIN_HUMAN Furin
4omc[36] O FMT
FORMIC ACID[3 atoms] 		A 100.0
/100.0		 3
/3		 FURIN_HUMAN Furin
6hlb[24] L DMS
DIMETHYL SULFOXIDE[4 atoms] 		A 100.0
/100.0		 5
/5		 FURIN_HUMAN Furin
7o1u[9] L DMS
DIMETHYL SULFOXIDE[4 atoms] 		A 100.0
/99.4		 2
/2		 FURIN_HUMAN Furin
7o1u[8] M DMS
DIMETHYL SULFOXIDE[4 atoms] 		A 100.0
/99.4		 3
/3		 FURIN_HUMAN Furin
7o1u[12] N DMS
DIMETHYL SULFOXIDE[4 atoms] 		A 100.0
/99.4		 3
/3		 FURIN_HUMAN Furin
7o1w[7] N DMS
DIMETHYL SULFOXIDE[4 atoms] 		A 100.0
/99.4		 5
/5		 FURIN_HUMAN Furin
7o1y[4] L DMS
DIMETHYL SULFOXIDE[4 atoms] 		A 100.0
/100.0		 3
/3		 FURIN_HUMAN Furin
7o1y[1] Q DMS
DIMETHYL SULFOXIDE[4 atoms] 		A 100.0
/100.0		 2
/2		 FURIN_HUMAN Furin
7qy1[1] Q DMS
DIMETHYL SULFOXIDE[4 atoms] 		A 100.0
/99.4		 1
/1		 FURIN_HUMAN Furin
6u9l[1] G SCN
THIOCYANATE ION[3 atoms] 		A 0.0
/50.7		 2
/2		 SUBTILISIN BPN'
1af4[1] E DIO
1,4-DIETHYLENE DIOXIDE[6 atoms] 		A 100.0
/49.2		 1
/4		 SUBT_BACLI SUBTILISIN CARLSBERG
1af4[3] G DIO
1,4-DIETHYLENE DIOXIDE[6 atoms] 		A 66.7
/49.2		 3
/5		 SUBT_BACLI SUBTILISIN CARLSBERG
1be6[1] E CCN
ACETONITRILE[3 atoms] 		A 0.0
/49.2		 2
/2		 SUBT_BACLI SUBTILISIN CARLSBERG
1be6[3] G CCN
ACETONITRILE[3 atoms] 		A 33.3
/49.2		 3
/3		 SUBT_BACLI SUBTILISIN CARLSBERG
1be6[2] J CCN
ACETONITRILE[3 atoms] 		A 0.0
/49.2		 1
/1		 SUBT_BACLI SUBTILISIN CARLSBERG
1be6[7] O CCN
ACETONITRILE[3 atoms] 		A 100.0
/49.2		 1
/3		 SUBT_BACLI SUBTILISIN CARLSBERG
1scb[4] G CCN
ACETONITRILE[3 atoms] 		A 33.3
/49.2		 3
/5		 SUBT_BACLI SUBTILISIN CARLSBERG
3lpc[1] E ACT
ACETATE ION[4 atoms] 		A 100.0
/32.6		 5
/6		 AprB2
3lpc[1] F ACT
ACETATE ION[4 atoms] 		A 100.0
/32.6		 2
/2		 AprB2
3lpc[1] G ACT
ACETATE ION[4 atoms] 		A 0.0
/32.6		 3
/3		 AprB2
3lpc[1] H ACT
ACETATE ION[4 atoms] 		A 0.0
/32.6		 4
/4		 AprB2
4hx2[1] S ACT
ACETATE ION[4 atoms] 		C 0.0
/49.2		 1
/5		 Q9FDF2_BACLI KerA
4hx2[1] L IPA
ISOPROPYL ALCOHOL[4 atoms] 		A 66.7
/49.2		 6
/6		 Q9FDF2_BACLI KerA
4hx2[1] U IPA
ISOPROPYL ALCOHOL[4 atoms] 		C 100.0
/49.2		 2
/3		 Q9FDF2_BACLI KerA
7am8[1] C AKR
ACRYLIC ACID[5 atoms] 		A 100.0
/48.6		 1
/6		 SUBT_BACAM Subtilisin BPN'
3bgo[2] C AZI
AZIDE ION[3 atoms] 		B 40.0
/47.1		 5
/8		 SUBT_BACAM Subtilisin BPN'
7am7[1] Q PGE
TRIETHYLENE GLYCOL[10 atoms] 		C 50.0
/47.1		 2
/4		 SUBT_BACAM Subtilisin BPN'
1c9j[10] B SO4
SULFATE ION[5 atoms] 		A 25.0
/37.0		 4
/4		 SUBS_BACLE SERINE PROTEASE
1p8j[11] AA SO4
SULFATE ION[5 atoms] 		A 100.0
/97.9		 4
/4		 FURI_MOUSE Furin precursor
1p8j[1] BA SO4
SULFATE ION[5 atoms] 		A 100.0
/97.9		 1
/1		 FURI_MOUSE Furin precursor
1p8j[12] CA SO4
SULFATE ION[5 atoms] 		A 100.0
/97.9		 4
/4		 FURI_MOUSE Furin precursor
1p8j[4] DA SO4
SULFATE ION[5 atoms] 		A 100.0
/97.9		 3
/3		 FURI_MOUSE Furin precursor
1p8j[1] EA SO4
SULFATE ION[5 atoms] 		A 100.0
/97.9		 3
/3		 FURI_MOUSE Furin precursor
1p8j[6] FA SO4
SULFATE ION[5 atoms] 		A 100.0
/97.9		 3
/3		 FURI_MOUSE Furin precursor
1p8j[1] JC SO4
SULFATE ION[5 atoms] 		A 100.0
/97.9		 1
/1		 FURI_MOUSE Furin precursor
1p8j[5] NA SO4
SULFATE ION[5 atoms] 		A 100.0
/97.9		 2
/2		 FURI_MOUSE Furin precursor
1p8j[17] V SO4
SULFATE ION[5 atoms] 		A 100.0
/97.9		 4
/4		 FURI_MOUSE Furin precursor
1p8j[2] X SO4
SULFATE ION[5 atoms] 		A 100.0
/97.9		 3
/3		 FURI_MOUSE Furin precursor
1p8j[7] Y SO4
SULFATE ION[5 atoms] 		A 100.0
/97.9		 1
/1		 FURI_MOUSE Furin precursor
1p8j[9] Z SO4
SULFATE ION[5 atoms] 		A 100.0
/97.9		 3
/3		 FURI_MOUSE Furin precursor
1p8j[1] MA SO4
SULFATE ION[5 atoms] 		B 100.0
/97.9		 3
/3		 FURI_MOUSE Furin precursor
1p8j[5] CB SO4
SULFATE ION[5 atoms] 		C 100.0
/97.9		 1
/1		 FURI_MOUSE Furin precursor
1p8j[2] FB SO4
SULFATE ION[5 atoms] 		D 100.0
/97.9		 3
/3		 FURI_MOUSE Furin precursor
1p8j[1] NB SO4
SULFATE ION[5 atoms] 		E 100.0
/97.9		 4
/4		 FURI_MOUSE Furin precursor
1p8j[1] EC SO4
SULFATE ION[5 atoms] 		F 50.0
/97.9		 2
/2		 FURI_MOUSE Furin precursor
1p8j[2] JC SO4
SULFATE ION[5 atoms] 		G 100.0
/97.9		 5
/5		 FURI_MOUSE Furin precursor
1p8j[2] SC SO4
SULFATE ION[5 atoms] 		H 100.0
/97.9		 2
/2		 FURI_MOUSE Furin precursor
1p8j[1] XC SO4
SULFATE ION[5 atoms] 		H 100.0
/97.9		 3
/3		 FURI_MOUSE Furin precursor
1wsd[1] C SO4
SULFATE ION[5 atoms] 		A 50.0
/37.0		 2
/3		 PRTM_BACSK M-protease
2b6n[1] D SO4
SULFATE ION[5 atoms] 		A 20.0
/29.7		 5
/5		 Q3HUQ2_9ENTR proteinase K
4c3v[1] C SO4
SULFATE ION[5 atoms] 		A 50.0
/49.2		 2
/3		 SUBT_BACLI SUBTILISIN CARLSBERG
4cfz[1] D SO4
SULFATE ION[5 atoms] 		A 0.0
/37.0		 2
/2		 SUBS_BACLE SUBTILISIN SAVINASE
4cfz[1] E SO4
SULFATE ION[5 atoms] 		A 0.0
/37.0		 2
/4		 SUBS_BACLE SUBTILISIN SAVINASE
7am7[2] M SO4
SULFATE ION[5 atoms] 		B 100.0
/47.1		 1
/4		 SUBT_BACAM Subtilisin BPN'
2sbt[1] B ACN
ACETONE[4 atoms] 		A 37.5
/43.3		 8
/8		 SUBT_BACAM SUBTILISIN NOVO
1tm1[16] E CIT
CITRIC ACID[13 atoms] 		A 100.0
/40.9		 1
/4		 SUBT_BACAM Subtilisin BPN' precursor
1tm1[21] H 1PE
PENTAETHYLENE GLYCOL[11 atoms] 		A 40.0
/40.9		 5
/5		 SUBT_BACAM Subtilisin BPN' precursor
1tm1[12] K 1PE
PENTAETHYLENE GLYCOL[14 atoms] 		A 16.7
/40.9		 6
/6		 SUBT_BACAM Subtilisin BPN' precursor
1tm7[4] K 1PE
PENTAETHYLENE GLYCOL[7 atoms] 		A 0.0
/40.9		 5
/5		 SUBT_BACAM Subtilisin BPN'
1gci[3] E GOL
GLYCEROL[6 atoms] 		A 100.0
/37.0		 2
/3		 SUBS_BACLE SUBTILISIN
1v5i[1] E GOL
GLYCEROL[6 atoms] 		A 66.7
/40.9		 3
/4		 SUBT_BACAM Subtilisin BPN'
1v5i[2] L GOL
GLYCEROL[6 atoms] 		A 66.7
/40.9		 3
/3		 SUBT_BACAM Subtilisin BPN'
1v5i[1] M GOL
GLYCEROL[6 atoms] 		A 0.0
/40.9		 1
/4		 SUBT_BACAM Subtilisin BPN'
3ti9[1] E GOL
GLYCEROL[6 atoms] 		A 12.5
/35.7		 8
/8		 Q46547_DICNO Serine protease
3unx[1] B GOL
GLYCEROL[6 atoms] 		A 0.0
/49.2		 2
/4		 SUBT_BACLI Subtilisin Carlsberg
3vyv[2] D GOL
GLYCEROL[6 atoms] 		A 75.0
/41.8		 4
/4		 SUBN_BACNA Subtilisin NAT
5aqe[2] F GOL
GLYCEROL[6 atoms] 		A 100.0
/37.0		 2
/4		 SUBS_BACLE SUBTILISIN SAVINASE
5arb[2] D GOL
GLYCEROL[6 atoms] 		A 16.7
/37.0		 6
/6		 SUBS_BACLE SUBTILISIN SAVINASE
5arb[2] E GOL
GLYCEROL[6 atoms] 		A 33.3
/37.0		 6
/6		 SUBS_BACLE SUBTILISIN SAVINASE
6u9l[4] E GOL
GLYCEROL[6 atoms] 		A 0.0
/50.7		 2
/4		 SUBTILISIN BPN'
6ube[2] J GOL
GLYCEROL[6 atoms] 		A 100.0
/47.1		 3
/3		 SUBTILISIN BPN'
8e7f[1] C GOL
GLYCEROL[6 atoms] 		A 0.0
/38.1		 1
/4		 PRTS_SERMA Extracellular serine protease
8ehe[1] J GOL
GLYCEROL[6 atoms] 		A 0.0
/33.6		 2
/2		 A0A0A7KVG3_TANFO Mirolase
8ehe[1] K GOL
GLYCEROL[6 atoms] 		A 33.3
/33.6		 6
/6		 A0A0A7KVG3_TANFO Mirolase
8ehe[1] L GOL
GLYCEROL[6 atoms] 		A 25.0
/33.6		 4
/5		 A0A0A7KVG3_TANFO Mirolase
8ehe[1] M GOL
GLYCEROL[6 atoms] 		A 100.0
/33.6		 1
/3		 A0A0A7KVG3_TANFO Mirolase
8ehe[1] S GOL
GLYCEROL[6 atoms] 		A 0.0
/33.6		 2
/2		 A0A0A7KVG3_TANFO Mirolase
4z2a[1] H EDO
1,2-ETHANEDIOL[4 atoms] 		A 100.0
/99.6		 5
/5		 FURIN_HUMAN Furin
6dwq[1] D EDO
1,2-ETHANEDIOL[4 atoms] 		A 50.0
/49.2		 2
/4		 Q9FDF2_BACLI KerA
6dwq[1] E EDO
1,2-ETHANEDIOL[4 atoms] 		A 0.0
/49.2		 4
/6		 Q9FDF2_BACLI KerA
6dwq[1] L EDO
1,2-ETHANEDIOL[4 atoms] 		A 33.3
/49.2		 3
/5		 Q9FDF2_BACLI KerA
6dwq[2] M EDO
1,2-ETHANEDIOL[4 atoms] 		A 66.7
/49.2		 3
/4		 Q9FDF2_BACLI KerA
6dwq[1] N EDO
1,2-ETHANEDIOL[4 atoms] 		A 0.0
/49.2		 2
/2		 Q9FDF2_BACLI KerA
6o44[1] F EDO
1,2-ETHANEDIOL[4 atoms] 		A 100.0
/41.8		 1
/3		 A0A024B5N4_BACIU Nattokinase
6uao[1] F EDO
1,2-ETHANEDIOL[4 atoms] 		A 100.0
/50.7		 1
/3		 SUBTILISIN BPN'
7lcu[1] G EDO
1,2-ETHANEDIOL[4 atoms] 		A 100.0
/99.1		 5
/5		 FURIN_HUMAN Furin
7lcu[1] H EDO
1,2-ETHANEDIOL[4 atoms] 		A 100.0
/99.1		 6
/6		 FURIN_HUMAN Furin
8ehe[1] P EDO
1,2-ETHANEDIOL[4 atoms] 		A 0.0
/33.6		 3
/3		 A0A0A7KVG3_TANFO Mirolase
8ehe[1] Q EDO
1,2-ETHANEDIOL[4 atoms] 		A 25.0
/33.6		 4
/4		 A0A0A7KVG3_TANFO Mirolase
3lpc[1] I PEG
DI(HYDROXYETHYL)ETHER[7 atoms] 		A 0.0
/32.6		 4
/4		 AprB2
4tr2[1] H PO4
PHOSPHATE ION[5 atoms] 		A 33.3
/45.8		 3
/6		 E6Y8B9_PLAVI Subtilisin-like 1 serine protease
4z2a[2] F PO4
PHOSPHATE ION[5 atoms] 		A 100.0
/99.6		 6
/6		 FURIN_HUMAN Furin
6hlb[11] J PO4
PHOSPHATE ION[5 atoms] 		A 100.0
/100.0		 5
/5		 FURIN_HUMAN Furin
6hlb[9] K PO4
PHOSPHATE ION[5 atoms] 		A 100.0
/100.0		 2
/2		 FURIN_HUMAN Furin
6yd4[2] K PO4
PHOSPHATE ION[5 atoms] 		A 100.0
/99.4		 3
/3		 FURIN_HUMAN Furin
8pol[2] G PO4
PHOSPHATE ION[5 atoms] 		A 0.0
/27.4		 1
/4		 SUB1_PLAF7 Subtilisin-like protease 1
8pol[1] M PO4
PHOSPHATE ION[5 atoms] 		B 33.3
/27.4		 3
/6		 SUB1_PLAF7 Subtilisin-like protease 1
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.