› 1zmt

X-ray diffraction
1.7Å resolution

Structure of haloalcohol dehalogenase HheC of Agrobacterium radiobacter AD1 in complex with (R)-para-nitro styrene oxide, with a water molecule in the halide-binding site

Released:
DOI: 10.2210/pdb1zmt/pdb
PDB entry 1zmt coloured by chain, front view.
PDB entry 1zmt coloured by chain, side view.
PDB entry 1zmt coloured by chain, top view.
Source organism: Agrobacterium tumefaciens
Primary publication:
Structural basis for the enantioselectivity of an epoxide ring opening reaction catalyzed by halo alcohol dehalogenase HheC.
de Jong RM, Tiesinga JJ, Villa A, Tang L, Janssen DB, Dijkstra BW
J Am Chem Soc 127 13338-43 (2005)
PMID: 16173767

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-571934 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Halohydrin dehalogenase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 254 amino acids
Theoretical weight: 27.98 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

1 bound ligand:
Ligand RNO 4 x RNO
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-2
Spacegroup: C2
Unit cell:
a: 146.444Å b: 72.041Å c: 97.42Å
α: 90° β: 92.88° γ: 90°
R-values:
R R work R free
0.202 0.199 0.224
Expression system: Escherichia coli BL21(DE3)

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Citations

6 review citations

Expanding the enzyme universe: accessing non-natural reactions by mechanism-guided directed evolution.
Renata et al. (2015)
5 more

2 mentions without citation

Recent advances on halohydrin dehalogenases-from enzyme identification to novel biocatalytic applications.
Schallmey et al. (2016)
1 more