3i4f

X-ray diffraction
2.39Å resolution

Structure of putative 3-oxoacyl-reductase from bacillus thuringiensis

Released:
Entry authors: Ramagopal UA, Kim J, Toro R, Burley SK, Almo SC, New York SGX Research Center for Structural Genomics (NYSGXRC)

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
PDBe Complex ID:
PDB-CPX-163645 (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: 264 amino acids
Theoretical weight: 29.6 KDa
Source organism: Bacillus thuringiensis serovar kurstaki str. T03a001
Expression system: Escherichia coli
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: NSLS BEAMLINE X29A
Spacegroup: P21
Unit cell:
a: 69.418Å b: 86.592Å c: 78.413Å
α: 90° β: 97.05° γ: 90°
R-values:
R R work R free
0.195 0.192 0.248
Expression system: Escherichia coli