3GCW

PCSK9:EGFA(H306Y)

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004252	molecular_function	serine-type endopeptidase activity
A	0006508	biological_process	proteolysis
A	0008236	molecular_function	serine-type peptidase activity
E	0005509	molecular_function	calcium ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA E 1

Chain	Residue
E	MET292
E	THR294
E	GLU296
E	ASP310
E	LEU311
E	GLY314

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Functional Information from PROSITE/UniProt

site_id	PS01186
Number of Residues	15
Details	EGF_2 EGF-like domain signature 2. ClCpdGFqlvaqrr.C

Chain	Residue	Details
E	CYS317-CYS331
E	CYS356-CYS371

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site_id	PS01187
Number of Residues	24
Details	EGF_CA Calcium-binding EGF-like domain signature. DiDECqdpdt.........Csql....CvNleggYkC

Chain	Residue	Details
E	ASP333-CYS356

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site_id	PS00010
Number of Residues	12
Details	ASX_HYDROXYL Aspartic acid and asparagine hydroxylation site. CnDlkigYeClC

Chain	Residue	Details
E	CYS308-CYS319
E	CYS347-CYS358

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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
A	ASP186
A	HIS226
A	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
A	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
A	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
A	ASN533

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