1fj8

X-ray diffraction
2.27Å resolution

THE STRUCTURE OF BETA-KETOACYL-[ACYL CARRIER PROTEIN] SYNTHASE I IN COMPLEX WITH CERULENIN, IMPLICATIONS FOR DRUG DESIGN

Released:

Function and Biology Details

Reaction catalysed:
Acyl-[acyl-carrier-protein] + malonyl-[acyl-carrier-protein] = 3-oxoacyl-[acyl-carrier-protein] + CO(2) + [acyl-carrier-protein]

Structure analysis Details

Assembly composition:
homo dimer (preferred)
PDBe Complex ID:
PDB-CPX-141812 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
3-oxoacyl-[acyl-carrier-protein] synthase 1 Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 406 amino acids
Theoretical weight: 42.66 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P0A953 (Residues: 1-406; Coverage: 100%)
Gene names: JW2320, b2323, fabB, fabC
Sequence domains:
Structure domains: Peroxisomal Thiolase; Chain A, domain 1

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ENRAF-NONIUS FR571
Spacegroup: P212121
Unit cell:
a: 59.227Å b: 139.585Å c: 212.228Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.234 0.23 0.265
Expression system: Escherichia coli