3fdu

X-ray diffraction
2Å resolution

Crystal structure of a putative enoyl-CoA hydratase/isomerase from Acinetobacter baumannii

Released:
Entry authors: Bonanno JB, Dickey M, Bain KT, Tang BK, Romero R, Wasserman S, Sauder JM, Burley SK, Almo SC, New York SGX Research Center for Structural Genomics (NYSGXRC)

Function and Biology Details

Biochemical function:
Biological process:
  • not assigned
Cellular component:

Structure analysis Details

Assembly composition:
homo trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-495654 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Enoyl-CoA hydratase Chains: A, B, C, D, E, F
Molecule details ›
Chains: A, B, C, D, E, F
Length: 266 amino acids
Theoretical weight: 28.99 KDa
Source organism: Acinetobacter baumannii ATCC 17978
Expression system: Escherichia coli
UniProt:
  • Canonical: A0A1E3M6I3 (Residues: 10-264; Coverage: 96%)
Gene name: AUO97_01630
Sequence domains: Enoyl-CoA hydratase/isomerase
Structure domains:

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 31-ID
Spacegroup: P21
Unit cell:
a: 84.584Å b: 71.731Å c: 132.885Å
α: 90° β: 91.36° γ: 90°
R-values:
R R work R free
0.229 0.226 0.283
Expression system: Escherichia coli