3emk

X-ray diffraction
2.5Å resolution

2.5A crystal structure of glucose/ribitol dehydrogenase from brucella melitensis

Released:
Source organism: Brucella melitensis
Entry author: Seattle Structural Genomics Center for Infectious Disease (SSGCID)

Function and Biology Details

Reaction catalysed:
(3R)-3-hydroxyacyl-[acyl-carrier-protein] + NADP(+) = 3-oxoacyl-[acyl-carrier-protein] + NADPH
Biochemical function:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
PDBe Complex ID:
PDB-CPX-174169 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
3-oxoacyl-[acyl-carrier-protein] reductase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 246 amino acids
Theoretical weight: 26.07 KDa
Source organism: Brucella melitensis
Expression system: Escherichia coli
UniProt:
  • Canonical: Q2YMG6 (Residues: 1-245; Coverage: 100%)
Gene names: BAB1_0483, fabG
Sequence domains: Enoyl-(Acyl carrier protein) reductase
Structure domains: NAD(P)-binding Rossmann-like Domain

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-007 HF
Spacegroup: P21212
Unit cell:
a: 99.489Å b: 147.939Å c: 63.892Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.204 0.201 0.268
Expression system: Escherichia coli