› 2c3d

X-ray diffraction
2.15Å resolution

2.15 Angstrom crystal structure of 2-ketopropyl coenzyme M oxidoreductase carboxylase with a coenzyme M disulfide bound at the active site

Released:
DOI: 10.2210/pdb2c3d/pdb
PDB entry 2c3d coloured by chain, front view.
PDB entry 2c3d coloured by chain, side view.
PDB entry 2c3d coloured by chain, top view.
Source organism: Xanthobacter autotrophicus Py2
Primary publication:
Mechanistic implications of the structure of the mixed-disulfide intermediate of the disulfide oxidoreductase, 2-ketopropyl-coenzyme M oxidoreductase/carboxylase.
Pandey AS, Nocek B, Clark DD, Ensign SA, Peters JW
Biochemistry 45 113-20 (2006)
PMID: 16388586

Function and Biology Details

Reaction catalysed: 
Coenzyme M + acetoacetate + NADP(+) = 2-oxopropyl-CoM + CO(2) + NADPH
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-176381 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
2-oxopropyl-CoM reductase, carboxylating Chains: A, B
Molecule details ›
Chains: A, B
Length: 523 amino acids
Theoretical weight: 57.41 KDa
Source organism: Xanthobacter autotrophicus Py2
UniProt:
  • Canonical: Q56839 (Residues: 1-523; Coverage: 100%)
Gene names: Xaut_4867, xecC
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand FAD 2 x FAD
1 bound ligand:
Ligand COM 4 x COM
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL9-1
Spacegroup: P21
Unit cell:
a: 87.79Å b: 60.05Å c: 105.63Å
α: 90° β: 99.91° γ: 90°
R-values:
R R work R free
0.203 0.203 0.239

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Citations

1 review citation

Getting a handle on the role of coenzyme M in alkene metabolism.
Krishnakumar et al. (2008)
6 other articles