4pn3

X-ray diffraction
2.15Å resolution

Crystal structure of 3-hydroxyacyl-CoA-dehydrogenase from Brucella melitensis

Released:
Source organism: Brucella melitensis 64/150
Entry authors: Lukacs CM, Abendroth J, Edwards TE, Lorimer D, Seattle Structural Genomics Center for Infectious Disease (SSGCID)

Function and Biology Details

Biochemical function:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
3-hydroxyacyl-CoA dehydrogenase Chains: A, B, C, D, E, F, G, H
Molecule details ›
Chains: A, B, C, D, E, F, G, H
Length: 263 amino acids
Theoretical weight: 27.32 KDa
Source organism: Brucella melitensis 64/150
Expression system: Escherichia coli
Structure domains: NAD(P)-binding Rossmann-like Domain

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 21-ID-F
Spacegroup: P43
Unit cell:
a: 72.84Å b: 72.84Å c: 350.41Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.237 0.236 0.264
Expression system: Escherichia coli