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1QFM

PROLYL OLIGOPEPTIDASE FROM PORCINE MUSCLE

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 SGL A 781
ChainResidue
ATYR473
ASER554
AASN555
AVAL580
ATRP595
AHIS680
AHOH838

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SGL A 782
ChainResidue
ATRP595
AARG643
AHOH838
AHOH1473
AHOH1586
ACSX255
AILE591

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SGM A 783
ChainResidue
ACYS78
AHIS79
APHE80
ATYR385
ASER386
AHOH1212
AHOH1460

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SGM A 784
ChainResidue
APRO443
ACYS532
AGLU535

site_idAC5
Number of Residues9
DetailsBINDING SITE FOR RESIDUE GOL A 790
ChainResidue
AILE118
ALEU119
ASER120
AASP121
AASP446
AASN522
AASN525
AHOH1163
AHOH1418

site_idAC6
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL A 791
ChainResidue
AALA226
AGLU227
APHE228
ATRP262
AILE276
ALYS281
AHOH1238
AHOH1529

site_idAC7
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL A 792
ChainResidue
ATRP150
AVAL151
AGLU169
AARG170
AVAL171
ASER197
AHOH1021

site_idAC8
Number of Residues11
DetailsBINDING SITE FOR RESIDUE GOL A 793
ChainResidue
APRO7
AASP8
AVAL9
ATRP30
AGLN38
AALA41
APHE42
AHOH929
AHOH959
AHOH1412
AHOH1507

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
Detailsa catalytic site defined by CSA, PubMed 9695945, 10716187, 11915948, 12202494, 12228249
ChainResidueDetails
AASP641
ASER554
AHIS680

site_idMCSA1
Number of Residues4
DetailsM-CSA 901
ChainResidueDetails
ALEU489electrostatic stabiliser
ALEU570covalent catalysis, proton shuttle (general acid/base)
AGLY661electrostatic stabiliser, modifies pKa
AILE700proton shuttle (general acid/base)

246905

PDB entries from 2025-12-31

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