› 5my0

X-ray diffraction
2.94Å resolution

KS-MAT DI-DOMAIN OF MOUSE FAS WITH MALONYL-COA

Released:
DOI: 10.2210/pdb5my0/pdb
PDB entry 5my0 coloured by chain, front view.
PDB entry 5my0 coloured by chain, side view.
PDB entry 5my0 coloured by chain, top view.
Source organism: Mus musculus
Primary publication:
Characterization of the Polyspecific Transferase of Murine Type I Fatty Acid Synthase (FAS) and Implications for Polyketide Synthase (PKS) Engineering.
Rittner A, Paithankar KS, Huu KV, Grininger M
ACS Chem Biol 13 723-732 (2018)
PMID: 29328619

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:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-148494 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Fatty acid synthase Chains: A, D
Molecule details ›
Chains: A, D
Length: 852 amino acids
Theoretical weight: 92.27 KDa
Source organism: Mus musculus
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P19096 (Residues: 2-852; Coverage: 34%)
Gene name: Fasn
Sequence domains:
Structure domains:
Fatty acid synthase Chains: B, C
Molecule details ›
Chains: B, C
Length: 852 amino acids
Theoretical weight: 92.19 KDa
Source organism: Mus musculus
Expression system: Escherichia coli
UniProt:
  • Canonical: P19096 (Residues: 2-852; Coverage: 34%)
Gene name: Fasn
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand COA 2 x COA

Cofactor: Ligand MLC 1 x MLC
No bound ligands
1 modified residue:
Ligand K5L 2 x K5L

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X06SA
Spacegroup: C2221
Unit cell:
a: 147.044Å b: 354.39Å c: 217.463Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.19 0.188 0.222
Expression systems:
  • Escherichia coli BL21(DE3)
  • Escherichia coli

Quick links

Citations

3 review citations

Engineering strategies for rational polyketide synthase design.
Klaus et al. (2018)
2 more

4 mentions without citation

Type I fatty acid synthase trapped in the octanoyl-bound state.
Rittner et al. (2020)
3 more