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2PMW

The Crystal Structure of Proprotein convertase subtilisin kexin type 9 (PCSK9)

Functional Information from GO Data
ChainGOidnamespacecontents
B0004252molecular_functionserine-type endopeptidase activity
B0006508biological_processproteolysis
B0008236molecular_functionserine-type peptidase activity
Functional Information from PDB Data
site_idAC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 A 301
ChainResidue
AGLN101
AARG104
AARG105

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 A 302
ChainResidue
AGLN90
AARG93
AHIS139

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
BHIS226
BASP186
BSER386

246031

PDB entries from 2025-12-10

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