3POW

Crystal structure of the globular domain of human calreticulin

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005509	molecular_function	calcium ion binding
A	0005783	cellular_component	endoplasmic reticulum
A	0006457	biological_process	protein folding
A	0051082	molecular_function	unfolded protein binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CA A 900

Chain	Residue
A	GLN26
A	LYS62
A	LYS64
A	ASP328

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Functional Information from PROSITE/UniProt

site_id	PS00803
Number of Residues	16
Details	CALRETICULIN_1 Calreticulin family signature 1. KhEQnidCGGGYVKLF

Chain	Residue	Details
A	LYS98-PHE113

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site_id	PS00804
Number of Residues	9
Details	CALRETICULIN_2 Calreticulin family signature 2. IMFGPDiCG

Chain	Residue	Details
A	ILE130-GLY138

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	BINDING: BINDING => ECO:0000269|PubMed:21423620, ECO:0000269|PubMed:27840680, ECO:0007744|PDB:3POS, ECO:0007744|PDB:3POW, ECO:0007744|PDB:5LK5

Chain	Residue	Details
A	GLN26
A	LYS62
A	LYS64
A	ASP328

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site_id	SWS_FT_FI2
Number of Residues	5
Details	BINDING: BINDING => ECO:0000250|UniProtKB:P14211

Chain	Residue	Details
A	TYR109
A	LYS111
A	TYR128
A	ASP135
A	ASP317

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site_id	SWS_FT_FI3
Number of Residues	2
Details	MOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861

Chain	Residue	Details
A	LYS48
A	LYS159

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site_id	SWS_FT_FI4
Number of Residues	1
Details	MOD_RES: N6-(2-hydroxyisobutyryl)lysine => ECO:0000269|PubMed:29192674

Chain	Residue	Details
A	LYS64

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

Chain	Residue	Details
A	ASN344

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