› 4fwb

X-ray diffraction
1.26Å resolution

Structure of Rhodococcus rhodochrous haloalkane dehalogenase mutant DhaA31 in complex with 1, 2, 3 - trichloropropane

Released:
DOI: 10.2210/pdb4fwb/pdb
PDB entry 4fwb coloured by chain, front view.
PDB entry 4fwb coloured by chain, side view.
PDB entry 4fwb coloured by chain, top view.
Source organism: Rhodococcus rhodochrous
Primary publication:
Crystallographic analysis of 1,2,3-trichloropropane biodegradation by the haloalkane dehalogenase DhaA31.
Lahoda M, Mesters JR, Stsiapanava A, Chaloupkova R, Kuty M, Damborsky J, Kuta Smatanova I
Acta Crystallogr D Biol Crystallogr 70 209-17 (2014)
PMID: 24531456

Function and Biology Details

Reaction catalysed: 
1-haloalkane + H(2)O = a primary alcohol + halide
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-141208 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Haloalkane dehalogenase Chain: A
Molecule details ›
Chain: A
Length: 292 amino acids
Theoretical weight: 33.34 KDa
Source organism: Rhodococcus rhodochrous
Expression system: Escherichia coli
UniProt:
  • Canonical: P0A3G2 (Residues: 4-293; Coverage: 99%)
Gene name: dhaA
Sequence domains: alpha/beta hydrolase fold
Structure domains: alpha/beta hydrolase

Ligands and Environments

2 bound ligands:
Ligand 3KP 1 x 3KP
Ligand CL 4 x CL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE X12
Spacegroup: P1
Unit cell:
a: 42.498Å b: 44.395Å c: 46.538Å
α: 115.32° β: 97.7° γ: 109.58°
R-values:
R R work R free
0.136 0.136 0.166
Expression system: Escherichia coli

Quick links

Citations

1 review citation

Properties and biotechnological applications of natural and engineered haloalkane dehalogenases.
Nagata et al. (2015)
3 other articles

1 mention without citation

A self-compartmentalizing hexamer serine protease from Pyrococcus horikoshii: substrate selection achieved through multimerization.
Menyhárd et al. (2013)