› 2e3j

X-ray diffraction
2.1Å resolution

The crystal structure of epoxide hydrolase B (Rv1938) from mycobacterium tuberculosis at 2.1 angstrom

Released:
DOI: 10.2210/pdb2e3j/pdb
PDB entry 2e3j coloured by chain, front view.
PDB entry 2e3j coloured by chain, side view.
PDB entry 2e3j coloured by chain, top view.
Source organism: Mycobacterium tuberculosis H37Rv
Primary publication:
The molecular structure of epoxide hydrolase B from Mycobacterium tuberculosis and its complex with a urea-based inhibitor.
Biswal BK, Morisseau C, Garen G, Cherney MM, Garen C, Niu C, Hammock BD, James MN
J Mol Biol 381 897-912 (2008)
PMID: 18585390

Function and Biology Details

Reaction catalysed: 
An epoxide + H(2)O = a glycol
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assemblies composition:
homo dimer
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-161150 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Epoxide hydrolase B Chain: A
Molecule details ›
Chain: A
Length: 356 amino acids
Theoretical weight: 39.31 KDa
Source organism: Mycobacterium tuberculosis H37Rv
Expression system: Escherichia coli
UniProt:
  • Canonical: P95276 (Residues: 2-356; Coverage: 100%)
Gene name: MT1988
Sequence domains: alpha/beta hydrolase fold
Structure domains: alpha/beta hydrolase

Ligands and Environments

1 bound ligand:
Ligand ACT 9 x ACT
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 8.3.1
Spacegroup: P41212
Unit cell:
a: 66.258Å b: 66.258Å c: 157.109Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.235 0.235 0.276
Expression system: Escherichia coli

Quick links

Citations

4 review citations

Gates of enzymes.
Gora et al. (2013)
3 more

4 mentions without citation

The evolutionarily conserved protein CG9186 is associated with lipid droplets, required for their positioning and for fat storage.
Thiel et al. (2013)
3 more