› 1mo9

X-ray diffraction
1.65Å resolution

NADPH DEPENDENT 2-KETOPROPYL COENZYME M OXIDOREDUCTASE/CARBOXYLASE COMPLEXED WITH 2-KETOPROPYL COENZYME M

Released:
DOI: 10.2210/pdb1mo9/pdb
PDB entry 1mo9 coloured by chain, front view.
PDB entry 1mo9 coloured by chain, side view.
PDB entry 1mo9 coloured by chain, top view.
Source organism: Xanthobacter autotrophicus Py2
Primary publication:
Structural basis for CO2 fixation by a novel member of the disulfide oxidoreductase family of enzymes, 2-ketopropyl-coenzyme M oxidoreductase/carboxylase.
Nocek B, Jang SB, Jeong MS, Clark DD, Ensign SA, Peters JW
Biochemistry 41 12907-13 (2002)
PMID: 12390015

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 KPC 2 x KPC
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL9-1
Spacegroup: P21
Unit cell:
a: 87.98Å b: 60.12Å c: 105.6Å
α: 90° β: 102.5° γ: 90°
R-values:
R R work R free
0.189 0.188 0.213

Quick links

Citations

2 review citations

Getting a handle on the role of coenzyme M in alkene metabolism.
Krishnakumar et al. (2008)
1 more

6 mentions without citation

Prediction of Protein Loop Conformations using the AGBNP Implicit Solvent Model and Torsion Angle Sampling.
Felts et al. (2008)
5 more