› 4e46

X-ray diffraction
1.26Å resolution

Structure of Rhodococcus rhodochrous haloalkane dehalogenase DhaA in complex with 2-propanol

Released:
DOI: 10.2210/pdb4e46/pdb
Model geometry
Fit model/data
PDB entry 4e46 coloured by chain, front view.
PDB entry 4e46 coloured by chain, side view.
PDB entry 4e46 coloured by chain, top view.
Source organism: Rhodococcus rhodochrous
Primary publication:
Expansion of access tunnels and active-site cavities influence activity of haloalkane dehalogenases in organic cosolvents.
Stepankova V, Khabiri M, Brezovsky J, Pavelka A, Sykora J, Amaro M, Minofar B, Prokop Z, Hof M, Ettrich R, Chaloupkova R, Damborsky J
Chembiochem 14 890-7 (2013)
PMID: 23564727

Function and Biology Details

Reaction catalysed: 
1-haloalkane + H(2)O = a primary alcohol + halide
Biochemical function:
Biological process:
Cellular component:
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: 296 amino acids
Theoretical weight: 33.7 KDa
Source organism: Rhodococcus rhodochrous
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P0A3G2 (Residues: 1-293; Coverage: 100%)
Gene name: dhaA
Sequence domains: alpha/beta hydrolase fold
Structure domains: alpha/beta hydrolase

Ligands and Environments

3 bound ligands:
Ligand IPA 1 x IPA
Ligand ACT 2 x ACT
Ligand CL 1 x CL
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: EMBL/DESY, HAMBURG BEAMLINE X12
Spacegroup: P1
Unit cell:
a: 42.646Å b: 44.48Å c: 46.334Å
α: 115.39° β: 98.05° γ: 109.4°
R-values:
R R work R free
0.112 0.112 not available
Expression system: Escherichia coli BL21

Quick links

Citations

3 review citations

Dehalogenases: From Improved Performance to Potential Microbial Dehalogenation Applications.
Ang et al. (2018)
2 more

9 mentions without citation

FireProt: web server for automated design of thermostable proteins.
Musil et al. (2017)
8 more