› 7a42

X-ray diffraction
1.75Å resolution

Function and Biology Details

Reaction catalysed: 
Haloacetate + H(2)O = glycolate + halide
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-179995 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Fluoroacetate dehalogenase Chains: A, B
Molecule details ›
Chains: A, B
Length: 306 amino acids
Theoretical weight: 34.07 KDa
Source organism: Rhodopseudomonas palustris
Expression system: Escherichia coli
UniProt:
  • Canonical: Q6NAM1 (Residues: 1-302; Coverage: 100%)
Gene name: RPA1163
Sequence domains: alpha/beta hydrolase fold

Ligands and Environments

1 bound ligand:
Ligand CL 2 x CL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PETRA III, EMBL c/o DESY BEAMLINE P14 (MX2)
Spacegroup: P21
Unit cell:
a: 41.9Å b: 79.9Å c: 84.8Å
α: 90° β: 103.4° γ: 90°
R-values:
R R work R free
0.158 0.157 0.193
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Mapping Enzyme Landscapes by Time-Resolved Crystallography with Synchrotron and X-Ray Free Electron Laser Light.
Wilson MA. (2022)
1 more

1 mention without citation

Serial femtosecond and serial synchrotron crystallography can yield data of equivalent quality: A systematic comparison.
Mehrabi et al. (2021)