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1QF2

THERMOLYSIN (E.C.3.4.24.27) COMPLEXED WITH (2-SULPHANYL-3-PHENYLPROPANOYL)-GLY-(5-PHENYLPROLINE). PARAMETERS FOR ZN-MONODENTATION OF MERCAPTOACYLDIPEPTIDES IN METALLOENDOPEPTIDASE

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 320
ChainResidue
AHIS142
AHIS146
AGLU166
ATI3317

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 321
ChainResidue
AASP185
AGLU187
AGLU190
AHOH331
AASP138
AGLU177

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 322
ChainResidue
AGLU177
AASN183
AASP185
AGLU190
AHOH341
AHOH351

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 323
ChainResidue
AASP57
AASP59
AGLN61
AHOH328
AHOH352
AHOH381

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 324
ChainResidue
ATYR193
ATHR194
AILE197
AASP200
AHOH350
AHOH380

site_idAC6
Number of Residues14
DetailsBINDING SITE FOR RESIDUE TI3 A 317
ChainResidue
AASN111
AASN112
APHE130
ALEU133
AVAL139
AHIS142
AGLU143
AGLU166
ALEU202
AARG203
AHIS231
AZN320
AHOH492
AHOH543

site_idAC7
Number of Residues2
DetailsBINDING SITE FOR RESIDUE DMS A 325
ChainResidue
ASER218
ATYR251

site_idAC8
Number of Residues2
DetailsBINDING SITE FOR RESIDUE DMS A 326
ChainResidue
ATRP115
AHIS146

site_idAC9
Number of Residues1
DetailsBINDING SITE FOR RESIDUE DMS A 327
ChainResidue
ATYR151

site_idZN
Number of Residues3
DetailsZN BINDING SITE
ChainResidue
AHIS146
AHIS142
AGLU166

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
DetailsActive site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU10095","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"4808703","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues1
DetailsActive site: {"description":"Proton donor","evidences":[{"source":"PROSITE-ProRule","id":"PRU10095","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"4808703","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues16
DetailsBinding site: {}
ChainResidueDetails

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 2025-12-24

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