4jfc

X-ray diffraction
2.25Å resolution

Crystal structure of a enoyl-CoA hydratase from Polaromonas sp. JS666

Released:
Source organism: Polaromonas sp. JS666
Entry authors: Kumaran D, Chamala S, Evans B, Foti R, Gizzi A, Hillerich B, Kar A, Lafleur J, Seidel R, Villigas G, Zencheck W, Al Obaidi N, Almo SC, Swaminathan S, New York Structural Genomics Research Consortium (NYSGRC)

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
Macromolecule:
Enoyl-CoA hydratase Chain: A
Molecule details ›
Chain: A
Length: 281 amino acids
Theoretical weight: 29.94 KDa
Source organism: Polaromonas sp. JS666
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q129C0 (Residues: 1-259; Coverage: 100%)
Gene name: Bpro_2958
Sequence domains: Enoyl-CoA hydratase/isomerase
Structure domains:

Ligands and Environments

1 bound ligand:
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X29A
Spacegroup: P63
Unit cell:
a: 111.182Å b: 111.182Å c: 41.17Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.17 0.168 0.211
Expression system: Escherichia coli BL21(DE3)