2W2Q

PCSK9-deltaC D374H mutant bound to WT EGF-A of LDLR

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	7
Details	BINDING SITE FOR RESIDUE CA E1333

Chain	Residue
E	THR294
E	GLU296
E	ASP310
E	LEU311
E	GLY314
E	HOH2007
E	HOH2010

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site_id	AC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA A1448

Chain	Residue
A	VAL333
A	THR335
A	CYS358
A	ASP360
A	ALA328
A	ALA330

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Functional Information from PROSITE/UniProt

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

---

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

---

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

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	3
Details	Active site: {"description":"Charge relay system","evidences":[{"source":"PROSITE-ProRule","id":"PRU01240","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	39
Details	Domain: {"description":"EGF-like 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00076","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI3
Number of Residues	72
Details	Domain: {"description":"Inhibitor I9","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

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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
A	HIS226
A	ASP186
A	SER386

---