› 1n61

X-ray diffraction
1.3Å resolution

Crystal Structure of the Cu,Mo-CO Dehydrogenase (CODH); Dithionite reduced state

Released:
DOI: 10.2210/pdb1n61/pdb
PDB entry 1n61 coloured by chain, front view.
PDB entry 1n61 coloured by chain, side view.
PDB entry 1n61 coloured by chain, top view.
Source organism: Afipia carboxidovorans OM5
Primary publication:
Catalysis at a dinuclear [CuSMo(==O)OH] cluster in a CO dehydrogenase resolved at 1.1-A resolution.
Dobbek H, Gremer L, Kiefersauer R, Huber R, Meyer O
Proc Natl Acad Sci U S A 99 15971-6 (2002)
PMID: 12475995

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: 88.85 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: 30.28 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
3 bound ligands:
Ligand PO4 1 x PO4
Ligand FES 4 x FES
Ligand CUN 2 x CUN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: MPG/DESY, HAMBURG BEAMLINE BW6
Spacegroup: P212121
Unit cell:
a: 119.162Å b: 131.375Å c: 160.318Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.145 0.142 0.184

Quick links

Citations

37 review citations

Frontiers, opportunities, and challenges in biochemical and chemical catalysis of CO2 fixation.
Appel et al. (2013)
36 more

1 mention without citation

Using neural networks and evolutionary information in decoy discrimination for protein tertiary structure prediction.
Tan et al. (2008)