› 4jcs

X-ray diffraction
1.77Å resolution

Crystal structure of Enoyl-CoA hydratase/isomerase from Cupriavidus metallidurans CH34

Released:
DOI: 10.2210/pdb4jcs/pdb
PDB entry 4jcs coloured by chain, front view.
PDB entry 4jcs coloured by chain, side view.
PDB entry 4jcs coloured by chain, top view.
Source organism: Cupriavidus metallidurans CH34
Entry authors: Eswaramoorthy S, Chamala S, Chamala B, Foti F, 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:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo hexamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-172942 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Enoyl-CoA hydratase/isomerase Chain: A
Molecule details ›
Chain: A
Length: 286 amino acids
Theoretical weight: 31.96 KDa
Source organism: Cupriavidus metallidurans CH34
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: Q1LBW6 (Residues: 1-264; Coverage: 100%)
Gene name: Rmet_5501
Sequence domains: Enoyl-CoA hydratase/isomerase
Structure domains:

Ligands and Environments

No bound ligands
1 modified residue:
Ligand MSE 9 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X29A
Spacegroup: R32
Unit cell:
a: 93.688Å b: 93.688Å c: 193.566Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.211 0.209 0.234
Expression system: Escherichia coli BL21

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