PDBe 1dd8

X-ray diffraction
2.3Å resolution

CRYSTAL STRUCTURE OF BETA-KETOACYL-[ACYL CARRIER PROTEIN] SYNTHASE I FROM ESCHERICHIA COLI

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]. 
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
homo dimer (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: 42.68 KDa
Source organism: 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

No bound ligands

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P212121
Unit cell:
a: 59.62Å b: 142.71Å c: 213.46Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.188 0.188 0.219