› 3i39

X-ray diffraction
1.36Å resolution

NI,FE-CODH-320 MV+CN state

Released:
DOI: 10.2210/pdb3i39/pdb
PDB entry 3i39 coloured by chain, front view.
PDB entry 3i39 coloured by chain, side view.
PDB entry 3i39 coloured by chain, top view.
Source organism: Carboxydothermus hydrogenoformans Z-2901
Primary publication:
Structural basis of cyanide inhibition of Ni, Fe-containing carbon monoxide dehydrogenase.
Jeoung JH, Dobbek H
J Am Chem Soc 131 9922-3 (2009)
PMID: 19583208

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 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: 1-636; Coverage: 100%)
Gene names: CHY_0085, cooS2, cooSII
Sequence domains: Prismane/CO dehydrogenase family
Structure domains:

Ligands and Environments

5 bound ligands:
Ligand SF4 1 x SF4
Ligand FES 1 x FES
Ligand WCC 1 x WCC
Ligand FE2 2 x FE2
Ligand CYN 1 x CYN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: BESSY BEAMLINE 14.2
Spacegroup: C2
Unit cell:
a: 111.279Å b: 75.834Å c: 71.099Å
α: 90° β: 111.33° γ: 90°
R-values:
R R work R free
0.156 0.154 0.19
Expression system: Escherichia coli

Quick links

Citations

10 review citations

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

3 mentions without citation

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