› 1zxi

X-ray diffraction
1.7Å resolution

Reconstituted CO dehydrogenase from Oligotropha carboxidovorans

Released:
DOI: 10.2210/pdb1zxi/pdb
PDB entry 1zxi coloured by chain, front view.
PDB entry 1zxi coloured by chain, side view.
PDB entry 1zxi coloured by chain, top view.
Source organism: Afipia carboxidovorans OM5
Primary publication:
Structural and functional reconstruction in situ of the [CuSMoO2] active site of carbon monoxide dehydrogenase from the carbon monoxide oxidizing eubacterium Oligotropha carboxidovorans.
Resch M, Dobbek H, Meyer O
J Biol Inorg Chem 10 518-28 (2005)
PMID: 16091936

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-148801 (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
Carbon monoxide dehydrogenase small chain Chains: A, D
Molecule details ›
Chains: A, D
Length: 166 amino acids
Theoretical weight: 17.81 KDa
Source organism: Afipia carboxidovorans OM5
UniProt:
  • Canonical: P19921 (Residues: 1-166; Coverage: 100%)
Gene names: OCA5_pHCG300300, coxS
Sequence domains:
Structure domains:
Carbon monoxide dehydrogenase large chain Chains: B, E
Molecule details ›
Chains: B, E
Length: 809 amino acids
Theoretical weight: 88.86 KDa
Source organism: Afipia carboxidovorans OM5
UniProt:
  • Canonical: P19919 (Residues: 1-809; Coverage: 100%)
Gene names: OCA5_pHCG300310, coxL
Sequence domains:
Structure domains:
Carbon monoxide dehydrogenase medium chain Chains: C, F
Molecule details ›
Chains: C, F
Length: 288 amino acids
Theoretical weight: 30.26 KDa
Source organism: Afipia carboxidovorans OM5
UniProt:
  • Canonical: P19920 (Residues: 1-288; Coverage: 100%)
Gene names: OCA5_pHCG300290, coxM
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand MCN 2 x MCN

Cofactor: Ligand FAD 2 x FAD
4 bound ligands:
Ligand PO4 1 x PO4
Ligand FES 4 x FES
Ligand CU 2 x CU
Ligand CUM 2 x CUM
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-2
Spacegroup: P212121
Unit cell:
a: 118.84Å b: 131.32Å c: 159.99Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.168 0.166 0.194

Quick links

Citations

5 review citations

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

3 mentions without citation

Structural, Mechanistic, and Functional Insights into an Arthrobacter nicotinovorans Molybdenum Hydroxylase Involved in Nicotine Degradation.
Wang et al. (2021)
2 more