1I0R

CRYSTAL STRUCTURE OF FERRIC REDUCTASE FROM ARCHAEOGLOBUS FULGIDUS

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0010181	molecular_function	FMN binding
A	0016491	molecular_function	oxidoreductase activity
A	0016723	molecular_function	oxidoreductase activity, acting on metal ions, NAD or NADP as acceptor
A	0042602	molecular_function	riboflavin reductase (NADPH) activity
A	0042803	molecular_function	protein homodimerization activity
A	0052851	molecular_function	ferric-chelate reductase (NADPH) activity
A	0140618	molecular_function	ferric-chelate reductase (NADH) activity
B	0000166	molecular_function	nucleotide binding
B	0010181	molecular_function	FMN binding
B	0016491	molecular_function	oxidoreductase activity
B	0016723	molecular_function	oxidoreductase activity, acting on metal ions, NAD or NADP as acceptor
B	0042602	molecular_function	riboflavin reductase (NADPH) activity
B	0042803	molecular_function	protein homodimerization activity
B	0052851	molecular_function	ferric-chelate reductase (NADPH) activity
B	0140618	molecular_function	ferric-chelate reductase (NADH) activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	23
Details	BINDING SITE FOR RESIDUE FMN A 2000

Chain	Residue
A	GLY26
A	ASN50
A	ASP51
A	THR52
A	GLY80
A	PHE81
A	ARG82
A	LYS83
A	SER84
A	LYS89
A	TYR150
A	GLN27
A	HOH2028
A	HOH2045
A	HOH2101
A	HOH2110
A	ILE28
A	ALA29
A	ASN30
A	THR31
A	CYS45
A	LEU46
A	ASN47

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	6
Details	BINDING: BINDING => ECO:0000269|PubMed:11525168, ECO:0007744|PDB:1I0S

Chain	Residue	Details
A	TYR7
A	HIS126
A	TYR147
B	TYR7
B	HIS126
B	TYR147

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site_id	SWS_FT_FI2
Number of Residues	8
Details	BINDING: BINDING => ECO:0000269|PubMed:11525168, ECO:0007744|PDB:1I0R, ECO:0007744|PDB:1I0S

Chain	Residue	Details
A	GLN27
A	CYS45
A	ARG82
A	LYS89
B	GLN27
B	CYS45
B	ARG82
B	LYS89

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