› 3b52

X-ray diffraction
1.5Å resolution

Ni,Fe-CODH-600 mV state + CO2

Released:
DOI: 10.2210/pdb3b52/pdb
PDB entry 3b52 coloured by chain, front view.
PDB entry 3b52 coloured by chain, side view.
PDB entry 3b52 coloured by chain, top view.
Source organism: Carboxydothermus hydrogenoformans Z-2901
Primary publication:
Carbon dioxide activation at the Ni,Fe-cluster of anaerobic carbon monoxide dehydrogenase.
Jeoung JH, Dobbek H
Science 318 1461-4 (2007)
PMID: 18048691

Function and Biology Details

Reaction catalysed: 
CO + H(2)O + 2 oxidized ferredoxin = CO(2) + 2 reduced ferredoxin + 2 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-190270 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Carbon monoxide dehydrogenase 2 Chain: X
Molecule details ›
Chain: X
Length: 656 amino acids
Theoretical weight: 69.19 KDa
Source organism: Carboxydothermus hydrogenoformans Z-2901
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9F8A8 (Residues: 4-636; Coverage: 100%)
Gene names: CHY_0085, cooS2, cooSII
Sequence domains: Prismane/CO dehydrogenase family
Structure domains:

Ligands and Environments

5 bound ligands:
Ligand FE2 1 x FE2
Ligand SF4 1 x SF4
Ligand FES 1 x FES
Ligand WCC 1 x WCC
Ligand CO2 1 x CO2
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ENRAF-NONIUS FR571
Spacegroup: C2
Unit cell:
a: 111.52Å b: 74.57Å c: 70.71Å
α: 90° β: 111.3° γ: 90°
R-values:
R R work R free
0.154 0.153 0.182
Expression system: Escherichia coli

Quick links

Citations

29 review citations

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

6 mentions without citation

Structure, function, and mechanism of the nickel metalloenzymes, CO dehydrogenase, and acetyl-CoA synthase.
Can et al. (2014)
5 more