› 3sk0

X-ray diffraction
1.78Å resolution

structure of Rhodococcus rhodochrous haloalkane dehalogenase DhaA mutant DhaA12

Released:
DOI: 10.2210/pdb3sk0/pdb
PDB entry 3sk0 coloured by chain, front view.
PDB entry 3sk0 coloured by chain, side view.
PDB entry 3sk0 coloured by chain, top view.
Source organism: Rhodococcus rhodochrous
Primary publication:
Dynamics and hydration explain failed functional transformation in dehalogenase design.
Sykora J, Brezovsky J, Koudelakova T, Lahoda M, Fortova A, Chernovets T, Chaloupkova R, Stepankova V, Prokop Z, Smatanova IK, Hof M, Damborsky J
Nat Chem Biol 10 428-30 (2014)
PMID: 24727901

Function and Biology Details

Reaction catalysed: 
1-haloalkane + H(2)O = a primary alcohol + halide
Biochemical function:
Biological process:
  • not assigned
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: 311 amino acids
Theoretical weight: 35.4 KDa
Source organism: Rhodococcus rhodochrous
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P0A3G2 (Residues: 1-141, 142-293; Coverage: 100%)
Gene name: dhaA
Sequence domains: alpha/beta hydrolase fold
Structure domains: alpha/beta hydrolase

Ligands and Environments

1 bound ligand:
Ligand CL 1 x CL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: BESSY BEAMLINE 14.1
Spacegroup: P212121
Unit cell:
a: 51.583Å b: 68.689Å c: 84.37Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.176 0.176 0.207
Expression system: Escherichia coli BL21

Quick links

Citations

5 review citations

Synthetic biology for the directed evolution of protein biocatalysts: navigating sequence space intelligently.
Currin et al. (2015)
4 more

1 mention without citation

Molecular Modeling of ABHD5 Structure and Ligand Recognition.
Shahoei et al. (2022)