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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 Residues3
DetailsACT_SITE: Charge relay system => ECO:0000255|PROSITE-ProRule:PRU01240
ChainResidueDetails
BASP186
BHIS226
BSER386

site_idSWS_FT_FI2
Number of Residues1
DetailsSITE: Cleavage; by furin and PCSK5 => ECO:0000269|PubMed:16912035
ChainResidueDetails
BARG218

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Phosphoserine; by FAM20C => ECO:0000269|PubMed:18498363, ECO:0000269|PubMed:26091039, ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163
ChainResidueDetails
BSER688

site_idSWS_FT_FI4
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16912035
ChainResidueDetails
BASN533

221051

PDB entries from 2024-06-12

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