4k2n

X-ray diffraction
2Å resolution

Crystal structure of an enoyl-CoA hydratase/ carnithine racemase from Magnetospirillum magneticum

Released:
Entry authors: Eswaramoorthy S, Chamala S, Evans 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

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

Structure analysis Details

Assembly composition:
homo trimer (preferred)
PDBe Complex ID:
PDB-CPX-174118 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Enoyl-CoA hydratase/carnithine racemase Chain: A
Molecule details ›
Chain: A
Length: 281 amino acids
Theoretical weight: 30.98 KDa
Source organism: Magnetospirillum magneticum AMB-1
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: Q2W7Q6 (Residues: 1-259; Coverage: 100%)
Gene name: amb1315
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: NSLS BEAMLINE X29A
Spacegroup: I23
Unit cell:
a: 120.31Å b: 120.31Å c: 120.31Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.228 0.195 0.212
Expression system: Escherichia coli BL21