› 4jjt

X-ray diffraction
2.5Å resolution

The crystal structure of enoyl-CoA hydratase from Mycobacterium tuberculosis H37Rv

Released:
DOI: 10.2210/pdb4jjt/pdb
PDB entry 4jjt coloured by chain, front view.
PDB entry 4jjt coloured by chain, side view.
PDB entry 4jjt coloured by chain, top view.
Source organism: Mycobacterium tuberculosis H37Rv
Entry authors: Tan K, Holowicki J, Endres M, Kim C-Y, Kim H, Hung L-W, Terwilliger TC, Joachimiak A, Midwest Center for Structural Genomics (MCSG), Structures of Mtb Proteins Conferring Susceptibility to Known Mtb Inhibitors (MTBI)

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo hexamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-125214 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Probable enoyl-CoA hydratase EchA16 (Enoyl hydrase) (Unsaturated acyl-CoA hydratase) (Crotonase) Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 252 amino acids
Theoretical weight: 27.07 KDa
Source organism: Mycobacterium tuberculosis H37Rv
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: I6YEH6 (Residues: 1-249; Coverage: 100%)
Gene names: Rv2831, echA16
Sequence domains: Enoyl-CoA hydratase/isomerase
Structure domains: 2-enoyl-CoA Hydratase; Chain A, domain 1

Ligands and Environments

2 bound ligands:
Ligand GOL 3 x GOL
Ligand ACT 1 x ACT
1 modified residue:
Ligand MSE 9 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: C2
Unit cell:
a: 130.318Å b: 86.874Å c: 80.957Å
α: 90° β: 126.02° γ: 90°
R-values:
R R work R free
0.182 0.18 0.227
Expression system: Escherichia coli BL21(DE3)

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