› 3vzp

X-ray diffraction
1.79Å resolution

Function and Biology Details

Reaction catalysed: 
(R)-3-hydroxyacyl-CoA + NADP(+) = 3-oxoacyl-CoA + NADPH
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-147031 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Acetoacetyl-CoA reductase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 257 amino acids
Theoretical weight: 27.67 KDa
Source organism: Cupriavidus necator H16
Expression system: Escherichia coli
UniProt:
  • Canonical: P14697 (Residues: 2-246; Coverage: 100%)
Gene names: H16_A1439, phaB, phbB
Sequence domains: short chain dehydrogenase
Structure domains: NAD(P)-binding Rossmann-like Domain

Ligands and Environments

3 bound ligands:
Ligand SO4 7 x SO4
Ligand GOL 2 x GOL
Ligand DIO 7 x DIO
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE BL-1A
Spacegroup: C2221
Unit cell:
a: 67.7Å b: 123.69Å c: 260.79Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.194 0.192 0.238
Expression system: Escherichia coli

Quick links

Citations

1 review citation

Beyond the outer limits of nature by directed evolution.
Molina-Espeja et al. (2016)
18 other articles

2 mentions without citation

Directed evolution and structural analysis of NADPH-dependent Acetoacetyl Coenzyme A (Acetoacetyl-CoA) reductase from Ralstonia eutropha reveals two mutations responsible for enhanced kinetics.
Matsumoto et al. (2013)
1 more