› 2kr5

Solution NMR

Solution Structure of an Acyl Carrier Protein Domain from Fungal Type I Polyketide Synthase

Released:
DOI: 10.2210/pdb2kr5/pdb
PDB entry 2kr5 coloured by chain, ensemble of 20 models, front view.
PDB entry 2kr5 coloured by chain, ensemble of 20 models, side view.
PDB entry 2kr5 coloured by chain, ensemble of 20 models, top view.
Source organism: Aspergillus parasiticus
Primary publication:
Solution structure of an acyl carrier protein domain from a fungal type I polyketide synthase.
Wattana-amorn P, Williams C, Płoskoń E, Cox RJ, Simpson TJ, Crosby J, Crump MP
Biochemistry 49 2186-93 (2010)
PMID: 20136099

Function and Biology Details

Reaction catalysed: 
7 malonyl-CoA + hexanoyl-[acyl-carrier protein] = 7 CoA + norsolorinate anthrone + [acyl-carrier protein] + 7 CO(2) + 2 H(2)O
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-171284 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Norsolorinic acid synthase Chain: A
Molecule details ›
Chain: A
Length: 89 amino acids
Theoretical weight: 9.43 KDa
Source organism: Aspergillus parasiticus
Expression system: Escherichia coli
UniProt:
  • Canonical: Q12053 (Residues: 1705-1791; Coverage: 4%)
Gene names: P875_00052995, aflC, pksA, pksL1
Sequence domains: Phosphopantetheine attachment site
Structure domains: ACP-like

Ligands and Environments

1 bound ligand:
Ligand PNS 1 x PNS
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: simulated annealing
Expression system: Escherichia coli

Quick links

Citations

3 review citations

Current understanding of fatty acid biosynthesis and the acyl carrier protein.
Chan et al. (2010)
2 more

6 mentions without citation

Structural analysis of protein-protein interactions in type I polyketide synthases.
Xu et al. (2013)
5 more