› 2cnr

Solution NMR

Structural studies on the interaction of ScFAS ACP with ACPS

Released:
DOI: 10.2210/pdb2cnr/pdb
PDB entry 2cnr coloured by chain, ensemble of 20 models, front view.
PDB entry 2cnr coloured by chain, ensemble of 20 models, side view.
PDB entry 2cnr coloured by chain, ensemble of 20 models, top view.
Source organism: Streptomyces coelicolor A3(2)
Primary publication:
Structure and malonyl CoA-ACP transacylase binding of streptomyces coelicolor fatty acid synthase acyl carrier protein.
Arthur CJ, Williams C, Pottage K, Płoskoń E, Findlow SC, Burston SG, Simpson TJ, Crump MP, Crosby J
ACS Chem Biol 4 625-36 (2009)
PMID: 19555075

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-159846 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Acyl carrier protein Chain: A
Molecule details ›
Chain: A
Length: 82 amino acids
Theoretical weight: 8.92 KDa
Source organism: Streptomyces coelicolor A3(2)
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P72393 (Residues: 1-82; Coverage: 100%)
Gene name: acpP
Sequence domains: Phosphopantetheine attachment site
Structure domains: ACP-like

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: ARIA
Expression system: Escherichia coli BL21(DE3)

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Citations

5 review citations

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