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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 Residues6
DetailsACT_SITE: Charge relay system => ECO:0000255|PROSITE-ProRule:PRU01240
ChainResidueDetails
PASP186
PHIS226
PSER386
AASP186
AHIS226
ASER386

site_idSWS_FT_FI2
Number of Residues2
DetailsSITE: Cleavage; by autolysis => ECO:0000269|PubMed:14622975
ChainResidueDetails
PGLN152
AGLN152

site_idSWS_FT_FI3
Number of Residues2
DetailsSITE: Cleavage; by furin and PCSK5 => ECO:0000269|PubMed:16912035
ChainResidueDetails
PARG218
AARG218

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: Sulfotyrosine => ECO:0000269|PubMed:16912035
ChainResidueDetails
PTYR38
ATYR38

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: Phosphoserine; by FAM20C => ECO:0000269|PubMed:18498363, ECO:0000269|PubMed:26091039
ChainResidueDetails
PSER47
ASER47

site_idSWS_FT_FI6
Number of Residues2
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
PSER688
ASER688

site_idSWS_FT_FI7
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16912035
ChainResidueDetails
PASN533
AASN533

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

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PDB entries from 2024-07-31

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