PDBe 3hhd

X-ray diffraction
2.15Å resolution

Structure of the Human Fatty Acid Synthase KS-MAT Didomain as a Framework for Inhibitor Design.

Released:

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Fatty acid synthase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 965 amino acids
Theoretical weight: 104.48 KDa
Source organism: Homo sapiens
Expression system: Spodoptera frugiperda
UniProt:
  • Canonical: P49327 (Residues: 2-963; Coverage: 38%)
Gene names: FAS, FASN
Sequence domains:
Structure domains: Alpha-Beta Plaits

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X10SA
Spacegroup: P1
Unit cell:
a: 86.62Å b: 91.16Å c: 132.11Å
α: 73.84° β: 86.83° γ: 62.54°
R-values:
R R work R free
0.171 0.169 0.211
Expression system: Spodoptera frugiperda