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3H42

Crystal structure of PCSK9 in complex with Fab from LDLR competitive antibody

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 Residues7
DetailsBINDING SITE FOR RESIDUE NA B 1
ChainResidue
BHOH106
BALA328
BALA330
BVAL333
BTHR335
BCYS358
BASP360

Functional Information from PROSITE/UniProt
site_idPS00290
Number of Residues7
DetailsIG_MHC Immunoglobulins and major histocompatibility complex proteins signature. YSCQVTH
ChainResidueDetails
LTYR196-HIS202
HTYR204-HIS210

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
DetailsSite: {"description":"Cleavage; by furin and PCSK5","evidences":[{"source":"PubMed","id":"16912035","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
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

246905

PDB entries from 2025-12-31

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