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1QF0

THERMOLYSIN (E.C.3.4.24.27) COMPLEXED WITH (2-SULPHANYL-3-PHENYLPROPANOYL)-PHE-TYR. PARAMETERS FOR ZN-BIDENTATION 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
ATI2317

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 321
ChainResidue
AASP185
AGLU187
AGLU190
AHOH327
AASP138
AGLU177

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE CA A 322
ChainResidue
AGLU177
ALYS182
AASN183
AASP185
AGLU190
AHOH348
AHOH351

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 323
ChainResidue
AASP57
AASP59
AGLN61
AHOH329
AHOH343
AHOH379

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 324
ChainResidue
ATYR193
ATHR194
AILE197
AASP200
AHOH335
AHOH384

site_idAC6
Number of Residues19
DetailsBINDING SITE FOR RESIDUE TI2 A 317
ChainResidue
AASN111
AASN112
AALA113
APHE114
AVAL139
AHIS142
AGLU143
AHIS146
ATYR157
AGLU166
AILE188
AGLY189
ALEU202
AARG203
AHIS231
AZN320
AHOH393
AHOH416
AHOH457

site_idAC7
Number of Residues2
DetailsBINDING SITE FOR RESIDUE DMS A 325
ChainResidue
AHIS146
AHOH352

site_idAC8
Number of Residues3
DetailsBINDING SITE FOR RESIDUE DMS A 326
ChainResidue
AHIS216
ASER218
ATYR251

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

240971

PDB entries from 2025-08-27

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