› 1qdb

X-ray diffraction
1.9Å resolution

CYTOCHROME C NITRITE REDUCTASE

Released:
DOI: 10.2210/pdb1qdb/pdb
PDB entry 1qdb coloured by chain, front view.
PDB entry 1qdb coloured by chain, side view.
PDB entry 1qdb coloured by chain, top view.
Source organism: Sulfurospirillum deleyianum
Primary publication:
Structure of cytochrome c nitrite reductase.
Einsle O, Messerschmidt A, Stach P, Bourenkov GP, Bartunik HD, Huber R, Kroneck PM
Nature 400 476-80 (1999)
PMID: 10440380

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-195577 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Cytochrome c-552 Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 473 amino acids
Theoretical weight: 53.38 KDa
Source organism: Sulfurospirillum deleyianum
UniProt:
  • Canonical: Q9Z4P4 (Residues: 42-514; Coverage: 96%)
Gene name: nrfA
Sequence domains: Cytochrome c552
Structure domains:

Ligands and Environments


Cofactor: Ligand HEC 15 x HEC
2 bound ligands:
Ligand CA 3 x CA
Ligand SO4 9 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: MPG/DESY, HAMBURG BEAMLINE BW6
Spacegroup: P21212
Unit cell:
a: 107.484Å b: 185.344Å c: 92.192Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.189 0.184 0.22

Quick links

Citations

33 review citations

Bacterial respiration: a flexible process for a changing environment.
Richardson DJ. (2000)
32 more

3 mentions without citation

Hidden relationships between metalloproteins unveiled by structural comparison of their metal sites.
Valasatava et al. (2015)
2 more