› 6ty7

X-ray diffraction
1.5Å resolution

Crystal structure of haloalkane dehalogenase variant DhaA115 domain-swapped dimer type-1

Released:
DOI: 10.2210/pdb6ty7/pdb
PDB entry 6ty7 coloured by chain, front view.
PDB entry 6ty7 coloured by chain, side view.
PDB entry 6ty7 coloured by chain, top view.
Source organism: synthetic construct
Primary publication:
Computational Enzyme Stabilization Can Affect Folding Energy Landscapes and Lead to Catalytically Enhanced Domain-Swapped Dimers
Markova K, Kunka A, Chmelova K, Havlasek M, Babkova P, Marques SM, Vasina M, Planas-Iglesias J, Chaloupkova R, Bednar D, Prokop Z, Damborsky J, Marek M
ACS Catalysis 11 12864-12885 (2021)

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:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-141209 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Haloalkane dehalogenase Chains: A, B
Molecule details ›
Chains: A, B
Length: 299 amino acids
Theoretical weight: 34.45 KDa
Source organism: synthetic construct
Expression system: Escherichia coli
UniProt:
  • Canonical: P0A3G2 (Residues: 1-293; Coverage: 100%)
Gene name: dhaA
Sequence domains: alpha/beta hydrolase fold

Ligands and Environments

5 bound ligands:
Ligand EDO 5 x EDO
Ligand MES 1 x MES
Ligand GOL 1 x GOL
Ligand PG4 1 x PG4
Ligand NO3 1 x NO3
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I04
Spacegroup: P212121
Unit cell:
a: 55.93Å b: 75.65Å c: 143.9Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.171 0.169 0.194
Expression system: Escherichia coli

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