› 2fac

X-ray diffraction
1.76Å resolution

Crystal structure of E. coli hexanoyl-ACP

Released:
DOI: 10.2210/pdb2fac/pdb
PDB entry 2fac coloured by chain, front view.
PDB entry 2fac coloured by chain, side view.
PDB entry 2fac coloured by chain, top view.
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
Assembly name:
PDBe Complex ID:
PDB-CPX-141273 (preferred)
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

Membrane lipid homeostasis in bacteria.
Zhang et al. (2008)
15 more

10 mentions without citation

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