5kjp

X-ray diffraction
1.8Å resolution

Crystal structure of enoyl-CoA hydratase from Mycobacterium tuberculosis H37Rv

Released:
Entry authors: Nocek B, Hatzos-Skintges C, Anderson WF, Joachimiak A, Center for Structural Genomics of Infectious Diseases (CSGID)

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

Assembly composition:
homo trimer (preferred)
PDBe Complex ID:
PDB-CPX-161218 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Probable enoyl-CoA hydratase EchA1 (Enoyl hydrase) (Unsaturated acyl-CoA hydratase) (Crotonase) Chain: A
Molecule details ›
Chain: A
Length: 265 amino acids
Theoretical weight: 27.86 KDa
Source organism: Mycobacterium tuberculosis H37Rv
Expression system: Escherichia coli
UniProt:
  • Canonical: P96404 (Residues: 1-262; Coverage: 100%)
Gene names: Rv0222, echA1
Sequence domains: Enoyl-CoA hydratase/isomerase
Structure domains:

Ligands and Environments

No bound ligands
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: I23
Unit cell:
a: 121.476Å b: 121.476Å c: 121.476Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.155 0.153 0.184
Expression system: Escherichia coli