3i47

X-ray diffraction
1.58Å resolution

CRYSTAL STRUCTURE OF putative enoyl CoA hydratase/isomerase (crotonase) from Legionella pneumophila subsp. pneumophila str. Philadelphia 1

Released:
Entry authors: Malashkevich VN, Toro R, Morano C, Sauder JM, Burley SK, Almo SC, New York SGX Research Center for Structural Genomics (NYSGXRC)

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:
monomeric (preferred)
homo trimer
PDBe Complex ID:
PDB-CPX-178648 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Enoyl CoA hydratase/isomerase (Crotonase) Chain: A
Molecule details ›
Chain: A
Length: 268 amino acids
Theoretical weight: 29.58 KDa
Source organism: Legionella pneumophila subsp. pneumophila str. Philadelphia 1
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q5ZUH0 (Residues: 20-276; Coverage: 91%)
Gene name: lpg1828
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: NSLS BEAMLINE X29A
Spacegroup: R32
Unit cell:
a: 124.596Å b: 124.596Å c: 150.395Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.168 0.168 0.179
Expression system: Escherichia coli BL21(DE3)