› 3q6j

X-ray diffraction
1.92Å resolution

Structural basis for carbon dioxide binding by 2-ketopropyl coenzyme M Oxidoreductase/Carboxylase

Released:
DOI: 10.2210/pdb3q6j/pdb
PDB entry 3q6j coloured by chain, front view.
PDB entry 3q6j coloured by chain, side view.
PDB entry 3q6j coloured by chain, top view.
Source organism: Xanthobacter autotrophicus Py2
Primary publication:
Structural basis for carbon dioxide binding by 2-ketopropyl coenzyme M oxidoreductase/carboxylase.
Pandey AS, Mulder DW, Ensign SA, Peters JW
FEBS Lett 585 459-64 (2011)
PMID: 21192936

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 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

Cofactor: Ligand NAP 2 x NAP
6 bound ligands:
Ligand KPC 1 x KPC
Ligand MG 2 x MG
Ligand BCT 2 x BCT
Ligand CO2 1 x CO2
Ligand ACN 1 x ACN
Ligand COM 1 x COM
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL9-1
Spacegroup: P21
Unit cell:
a: 88.466Å b: 59.803Å c: 105.463Å
α: 90° β: 102.28° γ: 90°
R-values:
R R work R free
0.167 0.164 0.221

Quick links

Citations

8 citation in other articles

Roles of the redox-active disulfide and histidine residues forming a catalytic dyad in reactions catalyzed by 2-ketopropyl coenzyme M oxidoreductase/carboxylase.
Kofoed et al. (2011)
7 more

1 mention without citation

The reactive form of a C-S bond-cleaving, CO2-fixing flavoenzyme.
Streit et al. (2019)