› 1mok

X-ray diffraction
2.8Å resolution

NADPH DEPENDENT 2-KETOPROPYL COENZYME M OXIDOREDUCTASE/CARBOXYLASE

Released:
DOI: 10.2210/pdb1mok/pdb
PDB entry 1mok coloured by chain, front view.
PDB entry 1mok coloured by chain, side view.
PDB entry 1mok 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, C, D
Molecule details ›
Chains: A, B, C, D
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 4 x FAD
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL9-1
Spacegroup: P1
Unit cell:
a: 65.6Å b: 87.5Å c: 100.7Å
α: 72° β: 73.4° γ: 69.81°
R-values:
R R work R free
0.24 0.225 0.277

Quick links

Citations

2 review citations

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

3 mentions without citation

Lipidic cubic phases as matrices for membrane protein crystallization.
Nollert P. (2004)
2 more