3M0C

The X-ray Crystal Structure of PCSK9 in Complex with the LDL receptor

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
C	0005509	molecular_function	calcium ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CA C 1001

Chain	Residue
C	THR294
C	GLU296
C	ASP310
C	LEU311
C	GLY314

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site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CA C 1002

Chain	Residue
C	ASP333
C	ASP335
C	LEU350
C	GLU351

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site_id	AC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CA C 1003

Chain	Residue
C	LYS273
C	ASN276
C	ASP280
C	ASP286
C	GLU287

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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
C	CYS308-CYS319
C	CYS347-CYS358

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

Chain	Residue	Details
C	CYS317-CYS331
C	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
C	ASP333-CYS356

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site_id	PS01209
Number of Residues	25
Details	LDLRA_1 LDL-receptor class A (LDLRA) domain signature. CIsykwv.CDgsaECqdg.SDEsqet.C

Chain	Residue	Details
C	CYS18-CYS42
C	CYS61-CYS83
C	CYS100-CYS122
C	CYS139-CYS163
C	CYS188-CYS210
C	CYS227-CYS249
C	CYS268-CYS292

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	766
Details	TOPO_DOM: Extracellular => ECO:0000250|UniProtKB:P01131

Chain	Residue	Details
C	ALA1-ARG767
B	HIS226
B	SER386

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site_id	SWS_FT_FI2
Number of Residues	1
Details	MOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P35952

Chain	Residue	Details
C	THR703

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site_id	SWS_FT_FI3
Number of Residues	2
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255

Chain	Residue	Details
C	ASN76
C	ASN494

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site_id	SWS_FT_FI4
Number of Residues	2
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19520913

Chain	Residue	Details
C	ASN135
C	ASN251

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site_id	SWS_FT_FI5
Number of Residues	1
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:12754519, ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19159218

Chain	Residue	Details
C	ASN636

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