3grp

X-ray diffraction
2.09Å resolution

2.1 Angstrom crystal structure of 3-ketoacyl-(acyl-carrier-protein) reductase from Bartonella henselae

Released:
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-102116 (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: 266 amino acids
Theoretical weight: 28.74 KDa
Source organism: Bartonella henselae str. Houston-1
Expression system: Escherichia coli
UniProt:
  • Canonical: A0A0H3LWT6 (Residues: 1-245; Coverage: 100%)
Gene names: BH05350, 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: ALS BEAMLINE 5.0.2
Spacegroup: P21
Unit cell:
a: 59.279Å b: 71.738Å c: 111.521Å
α: 90° β: 96.59° γ: 90°
R-values:
R R work R free
0.195 0.192 0.24
Expression system: Escherichia coli