› 1dub

X-ray diffraction
2.5Å resolution

2-ENOYL-COA HYDRATASE, DATA COLLECTED AT 100 K, PH 6.5

Released:
DOI: 10.2210/pdb1dub/pdb
PDB entry 1dub coloured by chain, front view.
PDB entry 1dub coloured by chain, side view.
PDB entry 1dub coloured by chain, top view.
Source organism: Rattus norvegicus
Primary publication:
Crystal structure of enoyl-coenzyme A (CoA) hydratase at 2.5 angstroms resolution: a spiral fold defines the CoA-binding pocket.
Engel CK, Mathieu M, Zeelen JP, Hiltunen JK, Wierenga RK
EMBO J 15 5135-45 (1996)
PMID: 8895557

Function and Biology Details

Reactions catalysed: 
(3S)-3-hydroxyacyl-CoA = trans-2(or 3)-enoyl-CoA + H(2)O
A (3E)-alk-3-enoyl-CoA = a (2E)-alk-2-enoyl-CoA
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo hexamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-146979 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Enoyl-CoA hydratase, mitochondrial Chains: A, B, C, D, E, F
Molecule details ›
Chains: A, B, C, D, E, F
Length: 261 amino acids
Theoretical weight: 28.32 KDa
Source organism: Rattus norvegicus
UniProt:
  • Canonical: P14604 (Residues: 30-290; Coverage: 90%)
Gene name: Echs1
Sequence domains: Enoyl-CoA hydratase/isomerase
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand CAA 5 x CAA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE X11
Spacegroup: P212121
Unit cell:
a: 75.972Å b: 93.635Å c: 246.818Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.209 0.209 0.265

Quick links

Citations

18 review citations

Divergent evolution of enzymatic function: mechanistically diverse superfamilies and functionally distinct suprafamilies.
Gerlt et al. (2001)
17 more

12 mentions without citation

Structural basis for channelling mechanism of a fatty acid beta-oxidation multienzyme complex.
Ishikawa et al. (2004)
11 more