› 3fbw

X-ray diffraction
1.23Å resolution

Structure of Rhodococcus rhodochrous haloalkane dehalogenase DhaA mutant C176Y

Released:
DOI: 10.2210/pdb3fbw/pdb
PDB entry 3fbw coloured by chain, front view.
PDB entry 3fbw coloured by chain, side view.
PDB entry 3fbw coloured by chain, top view.
Source organism: Rhodococcus rhodochrous
Primary publication:
Atomic resolution studies of haloalkane dehalogenases DhaA04, DhaA14 and DhaA15 with engineered access tunnels.
Stsiapanava A, Dohnalek J, Gavira JA, Kuty M, Koudelakova T, Damborsky J, Kuta Smatanova I
Acta Crystallogr D Biol Crystallogr 66 962-9 (2010)
PMID: 20823547

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: 299 amino acids
Theoretical weight: 34.17 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 BEZ 1 x BEZ
Ligand CL 6 x CL
Ligand MG 2 x MG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE X11
Spacegroup: P212121
Unit cell:
a: 42.678Å b: 76.294Å c: 93.098Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.137 0.136 0.167
Expression system: Escherichia coli BL21

Quick links

Citations

4 citation in other articles

Directed evolution strategies for enantiocomplementary haloalkane dehalogenases: from chemical waste to enantiopure building blocks.
van Leeuwen et al. (2012)
3 more

4 mentions without citation

Structure of the Saccharomyces cerevisiae Cet1-Ceg1 mRNA capping apparatus.
Gu et al. (2010)
3 more