› 4rf3

X-ray diffraction
1.69Å resolution

Crystal Structure of ketoreductase from Lactobacillus kefir, mutant A94F

Released:
DOI: 10.2210/pdb4rf3/pdb
PDB entry 4rf3 coloured by chain, front view.
PDB entry 4rf3 coloured by chain, side view.
PDB entry 4rf3 coloured by chain, top view.
Source organism: Lentilactobacillus kefiri
Primary publication:
Origins of stereoselectivity in evolved ketoreductases.
Noey EL, Tibrewal N, Jiménez-Osés G, Osuna S, Park J, Bond CM, Cascio D, Liang J, Zhang X, Huisman GW, Tang Y, Houk KN
Proc Natl Acad Sci U S A 112 E7065-72 (2015)
PMID: 26644568

Function and Biology Details

Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-180508 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
NADP-dependent (R)-specific alcohol dehydrogenase Chains: A, B
Molecule details ›
Chains: A, B
Length: 272 amino acids
Theoretical weight: 29.06 KDa
Source organism: Lentilactobacillus kefiri
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q6WVP7 (Residues: 1-252; Coverage: 100%)
Gene names: DNL43_05835, LKE01_04370, adh
Sequence domains: Enoyl-(Acyl carrier protein) reductase
Structure domains: NAD(P)-binding Rossmann-like Domain

Ligands and Environments

2 bound ligands:
Ligand MG 2 x MG
Ligand GOL 3 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 24-ID-C
Spacegroup: P21212
Unit cell:
a: 66.15Å b: 110.67Å c: 67.61Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.211 0.208 0.242
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

7 review citations

Power of Biocatalysis for Organic Synthesis.
Winkler et al. (2021)
6 more

1 mention without citation

Origins of stereoselectivity in evolved ketoreductases.
Noey et al. (2015)