X-ray diffraction
1.8Å resolution

1.8 Angstrom Resolution Crystal Structure of Enoyl-CoA Hydratase from Bacillus anthracis.

Source organism: Bacillus anthracis
Entry authors: Minasov G, Halavaty A, Wawrzak Z, Skarina T, Onopriyenko O, Papazisi L, Savchenko A, Anderson WF, Center for Structural Genomics of Infectious Diseases (CSGID)

Function and Biology Details

Reaction catalysed:
(3S)-3-hydroxyacyl-CoA = trans-2(or 3)-enoyl-CoA + H(2)O
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo trimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Enoyl-CoA hydratase/isomerase family protein Chains: A, B, C, D, E, F
Molecule details ›
Chains: A, B, C, D, E, F
Length: 265 amino acids
Theoretical weight: 29.1 KDa
Source organism: Bacillus anthracis
Expression system: Escherichia coli
  • Canonical: A0A6L8PDF4 (Residues: 1-262; Coverage: 100%)
Gene name: GBAA_2551
Sequence domains: Enoyl-CoA hydratase/isomerase
Structure domains:

Ligands and Environments

2 bound ligands:
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 21-ID-G
Spacegroup: P21
Unit cell:
a: 73.747Å b: 130.721Å c: 73.802Å
α: 90° β: 114.47° γ: 90°
R R work R free
0.157 0.156 0.193
Expression system: Escherichia coli