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1VZ2

PROLYL OLIGOPEPTIDASE FROM PORCINE BRAIN, Y73C/V427C/C255T MUTANT

Functional Information from GO Data
ChainGOidnamespacecontents
A0004252molecular_functionserine-type endopeptidase activity
A0005737cellular_componentcytoplasm
A0006508biological_processproteolysis
A0008233molecular_functionpeptidase activity
A0008236molecular_functionserine-type peptidase activity
A0016787molecular_functionhydrolase activity
Functional Information from PDB Data
site_idAC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL A 790
ChainResidue
AILE118
ASER120
AASP121
AASP446
AASN525
AHOH2419
AHOH2505

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL A 791
ChainResidue
AILE276
ALYS281
AHOH2506
AALA226
AGLU227

site_idAC3
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL A 793
ChainResidue
APRO568
AASP569
APHE571
AASP627
AILE628
AGLN629
APRO631
AASN668

site_idAC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL A 796
ChainResidue
AASP8
AVAL9
ATRP30
AGLN38
AALA41
APHE42
AHOH2186

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL A 798
ChainResidue
ATYR473
ASER554
AASN555
AHIS680
AHOH2472

Functional Information from PROSITE/UniProt
site_idPS00708
Number of Residues31
DetailsPRO_ENDOPEP_SER Prolyl endopeptidase family serine active site. DfqcAaeyLikegytspkrltinGgSnGGLL
ChainResidueDetails
AASP529-LEU559

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsActive site: {"description":"Charge relay system","evidences":[{"source":"PROSITE-ProRule","id":"PRU10084","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"1900195","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues1
DetailsActive site: {"description":"Charge relay system"}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues1
DetailsActive site: {"description":"Charge relay system","evidences":[{"source":"PROSITE-ProRule","id":"PRU10084","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"2064618","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues1
DetailsModified residue: {"description":"N-acetylmethionine","evidences":[{"source":"UniProtKB","id":"P48147","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues1
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P48147","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1pfq
ChainResidueDetails
AASP641
ASER554
AHIS680

site_idMCSA1
Number of Residues4
DetailsM-CSA 901
ChainResidueDetails
ATYR473electrostatic stabiliser
ASER554covalent catalysis, proton shuttle (general acid/base)
AASP641electrostatic stabiliser, modifies pKa
AHIS680proton shuttle (general acid/base)

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PDB entries from 2025-07-30

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