3NVJ

Crystal structure of the C143A/C166A mutant of Ero1p

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005783	cellular_component	endoplasmic reticulum
A	0015035	molecular_function	protein-disulfide reductase activity
A	0016972	molecular_function	thiol oxidase activity
A	0034975	biological_process	protein folding in endoplasmic reticulum
A	0071949	molecular_function	FAD binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE NEN A 501

Chain	Residue
A	GLN205
A	CYS208
A	MET258
A	ASN263
A	TYR420

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site_id	AC2
Number of Residues	20
Details	BINDING SITE FOR RESIDUE FAD A 1

Chain	Residue
A	THR189
A	GLY190
A	TYR191
A	GLY192
A	ALA196
A	ILE199
A	TRP200
A	TYR204
A	SER228
A	HIS231
A	ALA232
A	ILE234
A	ARG260
A	ARG267
A	MET347
A	CYS355
A	HOH10
A	ASP108
A	ARG187
A	PHE188

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site_id	AC3
Number of Residues	2
Details	BINDING SITE FOR RESIDUE CD A 432

Chain	Residue
A	GLU241
A	GLU408

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	ACT_SITE: Nucleophile => ECO:0000269|PubMed:15163408

Chain	Residue	Details
A	CYS352

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site_id	SWS_FT_FI2
Number of Residues	1
Details	ACT_SITE: ACT_SITE => ECO:0000269|PubMed:15163408

Chain	Residue	Details
A	CYS355

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site_id	SWS_FT_FI3
Number of Residues	6
Details	BINDING: BINDING => ECO:0000269|PubMed:15163408

Chain	Residue	Details
A	ARG187
A	THR189
A	TRP200
A	SER228
A	HIS231
A	ARG260

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site_id	SWS_FT_FI4
Number of Residues	2
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255

Chain	Residue	Details
A	ASN130
A	ASN342

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