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1E8N

PROLYL OLIGOPEPTIDASE FROM PORCINE BRAIN, MUTANT, COMPLEXED WITH PEPTIDE

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 Residues10
DetailsBINDING SITE FOR RESIDUE GOL A 790
ChainResidue
AILE118
AHOH2908
ALEU119
ASER120
AASP121
AASP446
AASN522
AASN525
AHOH2906
AHOH2907

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL A 791
ChainResidue
AALA226
AGLU227
APHE228
AILE276
ALYS281
AHOH2909
AHOH2910

site_idAC3
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL A 792
ChainResidue
ATRP150
AVAL151
ATHR152
AGLU169
AARG170
AVAL171
ASER197
AHOH2911

site_idAC4
Number of Residues10
DetailsBINDING SITE FOR RESIDUE GOL A 793
ChainResidue
APRO568
AASP569
APHE571
AGLY572
AILE628
AGLN629
APRO631
AASN668
AHOH2912
AHOH2913

site_idAC5
Number of Residues9
DetailsBINDING SITE FOR RESIDUE GOL A 794
ChainResidue
AGLU239
AASP291
ATYR292
AHOH2457
AHOH2462
AHOH2914
AHOH2915
AHOH2916
AHOH2917

site_idAC6
Number of Residues14
DetailsBINDING SITE FOR CHAIN I OF PEPTIDE INHIBITOR
ChainResidue
APHE173
ASER174
AGLY254
ATYR473
APHE476
AALA554
AASN555
AILE591
AALA594
ATRP595
AARG643
AHIS680
IHOH2002
IHOH2003

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 1qfm
ChainResidueDetails
AASP641
AALA554
AHIS680

site_idMCSA1
Number of Residues4
DetailsM-CSA 901
ChainResidueDetails
ATYR473electrostatic stabiliser
AALA554covalent catalysis, proton shuttle (general acid/base)
AASP641electrostatic stabiliser, modifies pKa
AHIS680proton shuttle (general acid/base)

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PDB entries from 2025-08-27

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