› 1gu6

X-ray diffraction
2.5Å resolution

Structure of the Periplasmic Cytochrome c Nitrite Reductase from Escherichia coli

Released:
DOI: 10.2210/pdb1gu6/pdb
PDB entry 1gu6 coloured by chain, front view.
PDB entry 1gu6 coloured by chain, side view.
PDB entry 1gu6 coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Structure and spectroscopy of the periplasmic cytochrome c nitrite reductase from Escherichia coli.
Bamford VA, Angove HC, Seward HE, Thomson AJ, Cole JA, Butt JN, Hemmings AM, Richardson DJ
Biochemistry 41 2921-31 (2002)
PMID: 11863430

Function and Biology Details

Reaction catalysed: 
NH(3) + 2 H(2)O + 6 ferricytochrome c = nitrite + 6 ferrocytochrome c + 7 H(+)
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-142181 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Cytochrome c-552 Chains: A, C, E, G
Molecule details ›
Chains: A, C, E, G
Length: 452 amino acids
Theoretical weight: 50.67 KDa
Source organism: Escherichia coli
UniProt:
  • Canonical: P0ABK9 (Residues: 27-478; Coverage: 100%)
Gene names: JW4031, b4070, nrfA
Sequence domains: Cytochrome c552
Structure domains:

Ligands and Environments


Cofactor: Ligand HEC 20 x HEC
2 bound ligands:
Ligand CA 8 x CA
Ligand GOL 4 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-1
Spacegroup: P212121
Unit cell:
a: 81.472Å b: 90.837Å c: 293.874Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.203 0.203 0.243

Quick links

Citations

8 review citations

Enzymology and bioenergetics of respiratory nitrite ammonification.
Simon J. (2002)
7 more

4 mentions without citation

The chemistry and biochemistry of heme c: functional bases for covalent attachment.
Bowman et al. (2008)
3 more