› 4ixt

X-ray diffraction
2.49Å resolution

Structure of a 37-fold mutant of halohydrin dehalogenase (HheC) bound to ethyl (R)-4-cyano-3-hydroxybutyrate

Released:
DOI: 10.2210/pdb4ixt/pdb
PDB 4ixt coloured by chain and viewed from the front.
PDB 4ixt coloured by chain and viewed from the side.
PDB 4ixt coloured by chain and viewed from the top.
Source organism: Agrobacterium tumefaciens
Primary publication:
Biocatalytic and structural properties of a highly engineered halohydrin dehalogenase.
Schallmey M, Floor RJ, Hauer B, Breuer M, Jekel PA, Wijma HJ, Dijkstra BW, Janssen DB
Chembiochem 14 870-81 (2013)
PMID: 23585096

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Halohydrin dehalogenase Chains: A, B
Molecule details ›
Chains: A, B
Length: 254 amino acids
Theoretical weight: 27.84 KDa
Source organism: Agrobacterium tumefaciens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q93D82 (Residues: 1-254; Coverage: 100%)
Gene name: hheC
Sequence domains: Enoyl-(Acyl carrier protein) reductase
Structure domains: NAD(P)-binding Rossmann-like Domain

Ligands and Environments

2 bound ligands:
Ligand 1H1 1 x 1H1
Ligand CL 1 x CL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-4
Spacegroup: P43212
Unit cell:
a: 104.682Å b: 104.682Å c: 121.191Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.26 0.199 0.249
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

4 review citations

Enzymatic Halogenation and Dehalogenation Reactions: Pervasive and Mechanistically Diverse.
Agarwal et al. (2017)
3 more

1 mention without citation

Enhancing the biocatalytic manufacture of the key intermediate of atorvastatin by focused directed evolution of halohydrin dehalogenase.
Luo et al. (2017)