4dry

X-ray diffraction
2.5Å resolution

The crystal structure of 3-oxoacyl-[acyl-carrier-protein] reductase from Rhizobium meliloti

Released:
Source organism: Sinorhizobium meliloti 1021
Entry authors: Zhang Z, Chamala S, Evans B, Foti R, Gizzi A, Hillerich B, Kar A, LaFleur J, Seidel R, Villigas G, Zencheck W, Almo SC, Swaminathan S, New York Structural Genomics Research Consortium (NYSGRC)

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo tetramer (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: 281 amino acids
Theoretical weight: 29.81 KDa
Source organism: Sinorhizobium meliloti 1021
Expression system: Escherichia coli
UniProt:
  • Canonical: Q92TX5 (Residues: 1-258; Coverage: 100%)
Gene name: SM_b20662
Sequence domains: short chain dehydrogenase
Structure domains: NAD(P)-binding Rossmann-like Domain

Ligands and Environments

1 bound ligand:
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X25
Spacegroup: P212121
Unit cell:
a: 86.531Å b: 98.128Å c: 117.22Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.209 0.206 0.264
Expression system: Escherichia coli