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X-ray diffraction
2.85Å resolution

Crystal Structure of Enoyl-CoA Hydratase from Thermus Thermophilus HB8

Released:
Source organism: Thermus thermophilus
Primary publication:
Crystal structure of enoyl-CoA hydratase from Thermus thermophilus HB8.
Acta Crystallogr F Struct Biol Commun 77 148-155 (2021)
PMID: 33949975

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 hexamer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Enoyl-CoA hydratase Chain: A
Molecule details ›
Chain: A
Length: 253 amino acids
Theoretical weight: 27.36 KDa
Source organism: Thermus thermophilus
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P83702 (Residues: 1-253; Coverage: 100%)
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: SPRING-8 BEAMLINE BL44B2
Spacegroup: R32
Unit cell:
a: 131.233Å b: 131.233Å c: 110.608Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.204 0.204 0.267
Expression system: Escherichia coli BL21(DE3)