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2G4Z

anomalous substructure of thermolysin

Functional Information from GO Data
ChainGOidnamespacecontents
A0004222molecular_functionmetalloendopeptidase activity
A0006508biological_processproteolysis
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 321
ChainResidue
AHIS142
AHIS146
AGLU166
ACL326

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 322
ChainResidue
AHOH395
AASP57
AASP59
AGLN61
AHOH367
AHOH382

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 323
ChainResidue
AASP138
AGLU177
AASP185
AGLU187
AGLU190
AHOH358

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 324
ChainResidue
ATYR193
ATHR194
AILE197
AASP200
AHOH339
AHOH356

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CL A 325
ChainResidue
AGLY12
ALEU14
AASP16
ALYS18

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CL A 326
ChainResidue
AHIS142
ATYR157
AGLU166
AHIS231
AZN321

site_idAC7
Number of Residues1
DetailsBINDING SITE FOR RESIDUE CL A 327
ChainResidue
AHOH412

site_idAC8
Number of Residues1
DetailsBINDING SITE FOR RESIDUE CL A 328
ChainResidue
AASP226

site_idAC9
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CL A 329
ChainResidue
AARG285
ALYS307

site_idBC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL A 330
ChainResidue
AARG260
AASP261
AHOH398

site_idBC2
Number of Residues1
DetailsBINDING SITE FOR RESIDUE CL A 331
ChainResidue
AARG260

site_idBC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 A 333
ChainResidue
AGLY3
ATHR4
ASER5
ATYR28
AASN60
AHOH352
AHOH394

Functional Information from PROSITE/UniProt
site_idPS00142
Number of Residues10
DetailsZINC_PROTEASE Neutral zinc metallopeptidases, zinc-binding region signature. VVAHELTHAV
ChainResidueDetails
AVAL139-VAL148

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10095, ECO:0000269|PubMed:4808703
ChainResidueDetails
AGLU143

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Proton donor => ECO:0000255|PROSITE-ProRule:PRU10095, ECO:0000269|PubMed:4808703
ChainResidueDetails
AHIS231

site_idSWS_FT_FI3
Number of Residues16
DetailsBINDING:
ChainResidueDetails
AASP57
AASP185
AGLU187
AGLU190
ATYR193
ATHR194
AILE197
AASP200
AASP59
AGLN61
AASP138
AHIS142
AHIS146
AGLU166
AGLU177
AASN183

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1tlp
ChainResidueDetails
AHIS231
AGLU143

site_idMCSA1
Number of Residues7
DetailsM-CSA 176
ChainResidueDetails
AHIS142metal ligand
AGLU143electrostatic stabiliser, metal ligand
AHIS146metal ligand
ATYR157electrostatic stabiliser, hydrogen bond donor, steric role
AGLU166metal ligand
AASP226activator, electrostatic stabiliser, hydrogen bond acceptor
AHIS231hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor

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PDB entries from 2025-06-11

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