› 3il4

X-ray diffraction
3Å resolution

Structure of E. faecalis FabH in complex with acetyl CoA

Released:
DOI: 10.2210/pdb3il4/pdb
PDB entry 3il4 coloured by chain, front view.
PDB entry 3il4 coloured by chain, side view.
PDB entry 3il4 coloured by chain, top view.
Source organism: Enterococcus faecalis
Primary publication:
Crystal structures of bacterial FabH suggest a molecular basis for the substrate specificity of the enzyme.
Gajiwala KS, Margosiak S, Lu J, Cortez J, Su Y, Nie Z, Appelt K
FEBS Lett 583 2939-46 (2009)
PMID: 19665020

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 analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-182633 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Beta-ketoacyl-[acyl-carrier-protein] synthase III Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 320 amino acids
Theoretical weight: 35.12 KDa
Source organism: Enterococcus faecalis
Expression system: Escherichia coli
UniProt:
  • Canonical: Q820T1 (Residues: 2-321; Coverage: 100%)
Gene names: EF_2885, fabH
Sequence domains:
Structure domains: Peroxisomal Thiolase; Chain A, domain 1

Ligands and Environments


Cofactor: Ligand ACO 4 x ACO
No bound ligands
1 modified residue:
Ligand CSO 8 x CSO

Experiments and Validation Details

Entry percentile scores
X-ray source: ENRAF-NONIUS FR591
Spacegroup: P21
Unit cell:
a: 66.751Å b: 93.295Å c: 104.254Å
α: 90° β: 93.9° γ: 90°
R-values:
R R work R free
0.196 0.196 0.27
Expression system: Escherichia coli

Quick links

Citations

3 review citations

Type II fatty acid and polyketide synthases: deciphering protein-protein and protein-substrate interactions.
Chen et al. (2018)
2 more