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2P4E

Crystal Structure of PCSK9

Functional Information from GO Data
ChainGOidnamespacecontents
A0004252molecular_functionserine-type endopeptidase activity
A0006508biological_processproteolysis
A0008236molecular_functionserine-type peptidase activity
P0004252molecular_functionserine-type endopeptidase activity
P0006508biological_processproteolysis
P0008236molecular_functionserine-type peptidase activity
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE HG P 693
ChainResidue
ATYR293
AHOH768
AHOH876
PCYS67
PSER147
PHG694

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE HG P 694
ChainResidue
PSER147
PHG693
PHOH723
AGLY292
AHOH876
PCYS67

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues72
DetailsDomain: {"description":"Inhibitor I9","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues3
DetailsActive site: {"description":"Charge relay system","evidences":[{"source":"PROSITE-ProRule","id":"PRU01240","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"16912035","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1sca
ChainResidueDetails
AHIS226
AASP186
ASER386

245396

PDB entries from 2025-11-26

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