4olq

X-ray diffraction
2.7Å resolution

Crystal Structure of a Putative enoyl-CoA hydratase/isomerase family protein from Hyphomonas neptunium

Released:
Entry authors: Szlachta K, Cooper DR, Chapman HC, Cymborowski MT, Stead M, Hillerich B, Ahmed M, Bonanno JB, Seidel R, Almo SC, Minor W, 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/isomerase family protein Chains: A, B, C, D, E, F
Molecule details ›
Chains: A, B, C, D, E, F
Length: 282 amino acids
Theoretical weight: 30.23 KDa
Source organism: Hyphomonas neptunium ATCC 15444
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q0C365 (Residues: 1-260; Coverage: 100%)
Gene name: HNE_1107
Sequence domains: Enoyl-CoA hydratase/isomerase
Structure domains:

Ligands and Environments

1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 21-ID-F
Spacegroup: P212121
Unit cell:
a: 62.595Å b: 122.39Å c: 210.232Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.232 0.23 0.261
Expression system: Escherichia coli BL21(DE3)