› 4e13

X-ray diffraction
2.08Å resolution

Substrate-directed dual catalysis of dicarbonyl compounds by diketoreductase

Released:
DOI: 10.2210/pdb4e13/pdb
PDB entry 4e13 coloured by chain, front view.
PDB entry 4e13 coloured by chain, side view.
PDB entry 4e13 coloured by chain, top view.
Source organism: Acinetobacter baylyi
Primary publication:
Dual catalysis mode for the dicarbonyl reduction catalyzed by diketoreductase.
Lu M, Huang Y, White MA, Wu X, Liu N, Cheng X, Chen Y
Chem Commun (Camb) 48 11352-4 (2012)
PMID: 23073461

Function and Biology Details

Reaction catalysed: 
(S)-3-hydroxyacyl-CoA + NAD(+) = 3-oxoacyl-CoA + NADH
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-109388 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
3-hydroxybutyryl-CoA dehydrogenase Chain: A
Molecule details ›
Chain: A
Length: 283 amino acids
Theoretical weight: 30.27 KDa
Source organism: Acinetobacter baylyi
UniProt:
  • Canonical: B1P3E1 (Residues: 1-283; Coverage: 100%)
Gene name: dkr
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand NAD 1 x NAD
3 bound ligands:
Ligand GOL 4 x GOL
Ligand 1PE 1 x 1PE
Ligand SO4 1 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU FR-E+ DW
Spacegroup: P6222
Unit cell:
a: 100.75Å b: 100.75Å c: 132.09Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.232 0.227 0.25

Quick links

Citations

1 citations in other articles

Crystal structure of 5-formyl-3-hydroxy-2-methylpyridine 4-carboxylic acid 5-dehydrogenase, an NAD⁺-dependent dismutase from Mesorhizobium loti.
Mugo et al. (2015)

4 mentions without citation

A Molecular Revolution in the Treatment of Hemophilia.
Butterfield et al. (2020)
3 more