Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

4AMY

PROLYL OLIGOPEPTIDASE FROM PORCINE BRAIN WITH A COVALENTLY BOUND INHIBITOR IC-1

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 Residues12
DetailsBINDING SITE FOR RESIDUE 2P2 A 791
ChainResidue
APHE173
AARG643
AVAL644
AHIS680
AMET235
AGLY254
ATYR473
APHE476
ASER554
AASN555
AVAL580
ATRP595

site_idAC2
Number of Residues9
DetailsBINDING SITE FOR RESIDUE GOL A 1711
ChainResidue
AILE118
ALEU119
ASER120
AASP121
AASP446
AASN525
AHOH2115
AHOH2339
AHOH2366

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL A 1712
ChainResidue
AALA226
AGLU227
ATRP262
AILE276
ALYS281
AHOH2433
AHOH2434

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL A 1713
ChainResidue
AGLU239
AASP291
ATYR292
AHOH2224
AHOH2227
AHOH2435

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_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)

238582

PDB entries from 2025-07-09

PDB statisticsPDBj update infoContact PDBjnumon