› 3wle

X-ray diffraction
2.16Å resolution

Crystal structure of (R)-carbonyl reductase from Candida Parapsilosis in complex with NAD

Released:
DOI: 10.2210/pdb3wle/pdb
PDB entry 3wle coloured by chain, front view.
PDB entry 3wle coloured by chain, side view.
PDB entry 3wle coloured by chain, top view.
Source organism: Candida parapsilosis
Primary publication:
Unconserved substrate-binding sites direct the stereoselectivity of medium-chain alcohol dehydrogenase.
Wang S, Nie Y, Xu Y, Zhang R, Ko TP, Huang CH, Chan HC, Guo RT, Xiao R
Chem Commun (Camb) 50 7770-2 (2014)
PMID: 24834985

Function and Biology Details

Reaction catalysed: 
A primary alcohol + NAD(+) = an aldehyde + NADH
Biochemical function:
Biological process:
  • not assigned
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-106738 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
alcohol dehydrogenase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 341 amino acids
Theoretical weight: 36.35 KDa
Source organism: Candida parapsilosis
Expression system: Escherichia coli
UniProt:
  • Canonical: A1X808 (Residues: 1-336; Coverage: 100%)
Gene names: CPRADH, rCR
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand NAD 4 x NAD
1 bound ligand:
Ligand ZN 8 x ZN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSRRC BEAMLINE BL13B1
Spacegroup: P212121
Unit cell:
a: 85.641Å b: 106.105Å c: 145.55Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.183 0.181 0.216
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Structural insights into alcohol dehydrogenases catalyzing asymmetric reductions.
An et al. (2019)
1 more

5 mentions without citation

Redesigning Enzymes for Biocatalysis: Exploiting Structural Understanding for Improved Selectivity.
Ding et al. (2022)
4 more