› 1i0r

X-ray diffraction
1.5Å resolution

CRYSTAL STRUCTURE OF FERRIC REDUCTASE FROM ARCHAEOGLOBUS FULGIDUS

Released:
DOI: 10.2210/pdb1i0r/pdb
PDB entry 1i0r coloured by chain, front view.
PDB entry 1i0r coloured by chain, side view.
PDB entry 1i0r coloured by chain, top view.
Source organism: Archaeoglobus fulgidus
Primary publication:
Crystal structures of a novel ferric reductase from the hyperthermophilic archaeon Archaeoglobus fulgidus and its complex with NADP+.
Chiu HJ, Johnson E, Schröder I, Rees DC
Structure 9 311-9 (2001)
PMID: 11525168

Function and Biology Details

Reaction catalysed: 
2 Fe(II)-siderophore + NAD(P)(+) + H(+) = 2 Fe(III)-siderophore + NAD(P)H
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-128126 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Ferric-chelate reductase (NAD(P)H) Chains: A, B
Molecule details ›
Chains: A, B
Length: 169 amino acids
Theoretical weight: 18.68 KDa
Source organism: Archaeoglobus fulgidus
Expression system: Escherichia coli
UniProt:
  • Canonical: O29428 (Residues: 1-169; Coverage: 100%)
Gene names: AF_0830, feR
Sequence domains: Flavin reductase like domain
Structure domains: Electron Transport, Fmn-binding Protein; Chain A

Ligands and Environments


Cofactor: Ligand FMN 1 x FMN
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL9-2
Spacegroup: P41212
Unit cell:
a: 56.378Å b: 56.378Å c: 214.57Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.206 0.205 0.22
Expression system: Escherichia coli

Quick links

Citations

5 review citations

Microbial ferric iron reductases.
Schröder et al. (2003)
4 more

2 mentions without citation

Characterization of a pseudomonad 2-nitrobenzoate nitroreductase and its catabolic pathway-associated 2-hydroxylaminobenzoate mutase and a chemoreceptor involved in 2-nitrobenzoate chemotaxis.
Iwaki et al. (2007)
1 more