2pbp

X-ray diffraction
1.8Å resolution

Crystal structure of ENOYL-CoA hydrates subunit I (gk_2039) from geobacillus kaustophilus HTA426

Released:
Entry authors: Jeyakanthan J, Kanaujia SP, Vasuki RC, Sekar K, Agari Y, Ebihara A, Kuramitsu S, Shinkai A, Shiro Y, Yokoyama S, RIKEN Structural Genomics/Proteomics Initiative (RSGI)

Function and Biology Details

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

Structure analysis Details

Assemblies composition:
homo dimer (preferred)
homo hexamer
PDBe Complex ID:
PDB-CPX-177385 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Enoyl-CoA hydratase subunit I (Phenylacetic acid catabolism) Chain: A
Molecule details ›
Chain: A
Length: 258 amino acids
Theoretical weight: 28.42 KDa
Source organism: Geobacillus kaustophilus HTA426
Expression system: Escherichia coli
UniProt:
  • Canonical: Q5KYB2 (Residues: 1-258; Coverage: 100%)
Gene name: GK2039
Sequence domains: Enoyl-CoA hydratase/isomerase
Structure domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL26B2
Spacegroup: P6322
Unit cell:
a: 75.801Å b: 75.801Å c: 137.06Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.174 0.174 0.207
Expression system: Escherichia coli