› 1b3n

X-ray diffraction
2.65Å resolution

BETA-KETOACYL CARRIER PROTEIN SYNTHASE AS A DRUG TARGET, IMPLICATIONS FROM THE CRYSTAL STRUCTURE OF A COMPLEX WITH THE INHIBITOR CERULENIN.

Released:
DOI: 10.2210/pdb1b3n/pdb
PDB entry 1b3n coloured by chain, front view.
PDB entry 1b3n coloured by chain, side view.
PDB entry 1b3n coloured by chain, top view.
Source organism: Escherichia coli K-12
Primary publication:
Structure of the complex between the antibiotic cerulenin and its target, beta-ketoacyl-acyl carrier protein synthase.
Moche M, Schneider G, Edwards P, Dehesh K, Lindqvist Y
J Biol Chem 274 6031-4 (1999)
PMID: 10037680

Function and Biology Details

Reaction catalysed: 
A (Z)-hexadec-9-enoyl-[acyl-carrier protein] + a malonyl-[acyl-carrier protein] = a (Z)-3-oxooctadec-11-enoyl-[acyl-carrier protein] + CO(2) + an [acyl-carrier protein]
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-141989 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
3-oxoacyl-[acyl-carrier-protein] synthase 2 Chain: A
Molecule details ›
Chain: A
Length: 412 amino acids
Theoretical weight: 42.96 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli
UniProt:
  • Canonical: P0AAI5 (Residues: 2-413; Coverage: 100%)
Gene names: JW1081, b1095, fabF, fabJ
Sequence domains:
Structure domains: Peroxisomal Thiolase; Chain A, domain 1

Ligands and Environments

1 bound ligand:
Ligand CER 1 x CER
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: MAX II BEAMLINE I711
Spacegroup: P3121
Unit cell:
a: 76.394Å b: 76.394Å c: 147.675Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.213 0.213 0.27
Expression system: Escherichia coli

Quick links

Citations

24 review citations

The structural biology of type II fatty acid biosynthesis.
White et al. (2005)
23 more

10 mentions without citation

Coupling between catalytic site and collective dynamics: a requirement for mechanochemical activity of enzymes.
Yang et al. (2005)
9 more