› 4w9n

X-ray diffraction
1.84Å resolution

Enoyl-acyl carrier protein-reductase domain from human fatty acid synthase complexed with triclosan

Released:
DOI: 10.2210/pdb4w9n/pdb
PDB entry 4w9n coloured by chain, front view.
PDB entry 4w9n coloured by chain, side view.
PDB entry 4w9n coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Crystal structure of the human fatty acid synthase enoyl-acyl carrier protein-reductase domain complexed with triclosan reveals allosteric protein-protein interface inhibition.
Sippel KH, Vyas NK, Zhang W, Sankaran B, Quiocho FA
J Biol Chem 289 33287-95 (2014)
PMID: 25301948

Function and Biology Details

Reactions catalysed: 
(3R)-3-hydroxyacyl-[acyl-carrier-protein] + NADP(+) = 3-oxoacyl-[acyl-carrier-protein] + NADPH
An acyl-[acyl-carrier protein] + NADP(+) = a trans-2,3-dehydroacyl-[acyl-carrier protein] + NADPH
Acetyl-CoA + [acyl-carrier-protein] = CoA + acetyl-[acyl-carrier-protein]
Malonyl-CoA + an [acyl-carrier-protein] = CoA + a malonyl-[acyl-carrier-protein]
Acyl-[acyl-carrier-protein] + malonyl-[acyl-carrier-protein] = 3-oxoacyl-[acyl-carrier-protein] + CO(2) + [acyl-carrier-protein]
Acetyl-CoA + n malonyl-CoA + 2n NADPH = a long-chain fatty acid + (n+1) CoA + n CO(2) + 2n NADP(+)
Oleoyl-[acyl-carrier-protein] + H(2)O = [acyl-carrier-protein] + oleate
A (3R)-3-hydroxyacyl-[acyl-carrier protein] = a trans-2-enoyl-[acyl-carrier protein] + H(2)O
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assemblies composition:
homo dimer
hetero dimer (preferred)
hetero tetramer
Assembly name:
PDBe Complex ID:
PDB-CPX-155923 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Fatty acid synthase Chains: A, B, D
Molecule details ›
Chains: A, B, D
Length: 339 amino acids
Theoretical weight: 36.78 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P49327 (Residues: 1529-1867; Coverage: 14%)
Gene names: FAS, FASN
Sequence domains: Zinc-binding dehydrogenase
Structure domains:
Fatty acid synthase Chain: C
Molecule details ›
Chain: C
Length: 339 amino acids
Theoretical weight: 36.84 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P49327 (Residues: 1529-1867; Coverage: 14%)
Gene names: FAS, FASN
Sequence domains: Zinc-binding dehydrogenase
Structure domains:

Ligands and Environments

4 bound ligands:
Ligand IMD 4 x IMD
Ligand CL 5 x CL
Ligand NA 4 x NA
Ligand TCL 2 x TCL
1 modified residue:
Ligand CCS 1 x CCS

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU FR-E+ SUPERBRIGHT
Spacegroup: P1
Unit cell:
a: 68.564Å b: 75.834Å c: 83.264Å
α: 65.38° β: 88.87° γ: 65.08°
R-values:
R R work R free
0.206 0.206 0.233
Expression system: Escherichia coli

Quick links

Citations

2 review citations

The architectures of iterative type I PKS and FAS.
Herbst et al. (2018)
1 more

2 mentions without citation

Crystal structure of the human fatty acid synthase enoyl-acyl carrier protein-reductase domain complexed with triclosan reveals allosteric protein-protein interface inhibition.
Sippel et al. (2014)
1 more