› 2fac

X-ray diffraction
1.76Å resolution

Crystal structure of E. coli hexanoyl-ACP

Released:
DOI: 10.2210/pdb2fac/pdb
PDB 2fac coloured by chain and viewed from the front.
PDB 2fac coloured by chain and viewed from the side.
PDB 2fac coloured by chain and viewed from the top.
Source organism: Escherichia coli
Primary publication:
Structural studies of fatty acyl-(acyl carrier protein) thioesters reveal a hydrophobic binding cavity that can expand to fit longer substrates.
Roujeinikova A, Simon WJ, Gilroy J, Rice DW, Rafferty JB, Slabas AR
J. Mol. Biol. 365 135-45 (2007)
PMID: 17059829

Function and Biology Details

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

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo tetramer
homo dimer
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Acyl carrier protein Chains: A, B
Molecule details ›
Chains: A, B
Length: 77 amino acids
Theoretical weight: 8.51 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P0A6A8 (Residues: 2-78; Coverage: 99%)
Gene names: JW1080, acpP, b1094
Sequence domains: Phosphopantetheine attachment site
Structure domains: ACP-like

Ligands and Environments

2 bound ligands:
Ligand ZN 11 x ZN
Ligand PM4 2 x PM4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-2
Spacegroup: P21212
Unit cell:
a: 48.414Å b: 105.045Å c: 27.927Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.184 0.184 0.241
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

16 review citations

Enzymology of standalone elongating ketosynthases.
Chen et al. (2022)
15 more

9 mentions without citation

Fatty acid biosynthesis revisited: structure elucidation and metabolic engineering.
Beld et al. (2015)
8 more