2PMW

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

Functional Information from GO Data

Chain	GOid	namespace	contents
B	0004252	molecular_function	serine-type endopeptidase activity
B	0006508	biological_process	proteolysis
B	0008236	molecular_function	serine-type peptidase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SO4 A 301

Chain	Residue
A	GLN101
A	ARG104
A	ARG105

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site_id	AC2
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SO4 A 302

Chain	Residue
A	GLN90
A	ARG93
A	HIS139

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	3
Details	ACT_SITE: Charge relay system => ECO:0000255|PROSITE-ProRule:PRU01240

Chain	Residue	Details
B	ASP186
B	HIS226
B	SER386

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site_id	SWS_FT_FI2
Number of Residues	1
Details	SITE: Cleavage; by furin and PCSK5 => ECO:0000269|PubMed:16912035

Chain	Residue	Details
B	ARG218

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site_id	SWS_FT_FI3
Number of Residues	1
Details	MOD_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

Chain	Residue	Details
B	SER688

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site_id	SWS_FT_FI4
Number of Residues	1
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16912035

Chain	Residue	Details
B	ASN533

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Catalytic Information from CSA

site_id	CSA1
Number of Residues	3
Details	Annotated By Reference To The Literature 1sca

Chain	Residue	Details
B	HIS226
B	ASP186
B	SER386

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