› 1ffu

X-ray diffraction
2.35Å resolution

CARBON MONOXIDE DEHYDROGENASE FROM HYDROGENOPHAGA PSEUDOFLAVA WHICH LACKS THE MO-PYRANOPTERIN MOIETY OF THE MOLYBDENUM COFACTOR

Released:
DOI: 10.2210/pdb1ffu/pdb
PDB entry 1ffu coloured by chain, front view.
PDB entry 1ffu coloured by chain, side view.
PDB entry 1ffu coloured by chain, top view.
Source organism: Hydrogenophaga pseudoflava
Primary publication:
The effect of intracellular molybdenum in Hydrogenophaga pseudoflava on the crystallographic structure of the seleno-molybdo-iron-sulfur flavoenzyme carbon monoxide dehydrogenase.
Hänzelmann P, Dobbek H, Gremer L, Huber R, Meyer O
J Mol Biol 301 1221-35 (2000)
PMID: 10966817

Function and Biology Details

Reaction catalysed: 
CO + a quinone + H(2)O = CO(2) + a quinol
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
hetero hexamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-148800 (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
Carbon monoxide dehydrogenase small chain Chains: A, D
Molecule details ›
Chains: A, D
Length: 163 amino acids
Theoretical weight: 17.75 KDa
Source organism: Hydrogenophaga pseudoflava
UniProt:
  • Canonical: P19915 (Residues: 1-163; Coverage: 100%)
Gene name: cutS
Sequence domains:
Structure domains:
Carbon monoxide dehydrogenase large chain Chains: B, E
Molecule details ›
Chains: B, E
Length: 803 amino acids
Theoretical weight: 87.35 KDa
Source organism: Hydrogenophaga pseudoflava
UniProt:
  • Canonical: P19913 (Residues: 1-803; Coverage: 100%)
Gene name: cutL
Sequence domains:
Structure domains:
Carbon monoxide dehydrogenase medium chain Chains: C, F
Molecule details ›
Chains: C, F
Length: 287 amino acids
Theoretical weight: 30.44 KDa
Source organism: Hydrogenophaga pseudoflava
UniProt:
  • Canonical: P19914 (Residues: 1-287; Coverage: 100%)
Gene name: cutM
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand FAD 2 x FAD
2 bound ligands:
Ligand FES 4 x FES
Ligand CDP 2 x CDP
2 modified residues:
Ligand ARO 2 x ARO
Ligand CSZ 2 x CSZ

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU
Spacegroup: P212121
Unit cell:
a: 87.235Å b: 193.884Å c: 218.29Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.208 0.208 0.245

Quick links

Citations

11 review citations

The mononuclear molybdenum enzymes.
Hille et al. (2014)
10 more

4 mentions without citation

The many faces of protein-protein interactions: A compendium of interface geometry.
Kim et al. (2006)
3 more