› 2eft

X-ray diffraction
2Å resolution

Methanethiol-CYS 112 inhibition complex of E. coli ketoacyl synthase III (FABH) and Coenzyme A (high concentration (1.7mM) soak)

Released:
DOI: 10.2210/pdb2eft/pdb
PDB entry 2eft coloured by chain, front view.
PDB entry 2eft coloured by chain, side view.
PDB entry 2eft coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Alkyl-CoA disulfides as inhibitors and mechanistic probes for FabH enzymes.
Alhamadsheh MM, Musayev F, Komissarov AA, Sachdeva S, Wright HT, Scarsdale N, Florova G, Reynolds KA
Chem Biol 14 513-24 (2007)
PMID: 17524982

Function and Biology Details

Reaction catalysed: 
Acetyl-CoA + malonyl-[acyl-carrier-protein] = acetoacetyl-[acyl-carrier-protein] + CoA + CO(2)
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-141418 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Beta-ketoacyl-[acyl-carrier-protein] synthase III Chains: A, B
Molecule details ›
Chains: A, B
Length: 317 amino acids
Theoretical weight: 33.55 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P0A6R0 (Residues: 1-317; Coverage: 100%)
Gene names: JW1077, b1091, fabH
Sequence domains:
Structure domains: Peroxisomal Thiolase; Chain A, domain 1

Ligands and Environments


Cofactor: Ligand COA 1 x COA
2 bound ligands:
Ligand SO4 2 x SO4
Ligand MEE 2 x MEE
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU
Spacegroup: P212121
Unit cell:
a: 64.212Å b: 81.216Å c: 123.36Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.199 0.197 0.246
Expression system: Escherichia coli

Quick links

Citations

8 review citations

Bacterial lipids: metabolism and membrane homeostasis.
Parsons et al. (2013)
7 more

5 mentions without citation

The Mycobacterium tuberculosis beta-ketoacyl-acyl carrier protein synthase III activity is inhibited by phosphorylation on a single threonine residue.
Veyron-Churlet et al. (2009)
4 more