› 1l0h

X-ray diffraction
2Å resolution

CRYSTAL STRUCTURE OF BUTYRYL-ACP FROM E.COLI

Released:
DOI: 10.2210/pdb1l0h/pdb
PDB entry 1l0h coloured by chain, front view.
PDB entry 1l0h coloured by chain, side view.
PDB entry 1l0h coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
X-ray crystallographic studies on butyryl-ACP reveal flexibility of the structure around a putative acyl chain binding site.
Roujeinikova A, Baldock C, Simon WJ, Gilroy J, Baker PJ, Stuitje AR, Rice DW, Slabas AR, Rafferty JB
Structure 10 825-35 (2002)
PMID: 12057197

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-141273 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Acyl carrier protein Chain: A
Molecule details ›
Chain: A
Length: 78 amino acids
Theoretical weight: 8.65 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P0A6A8 (Residues: 1-78; Coverage: 100%)
Gene names: JW1080, acpP, b1094
Sequence domains: Phosphopantetheine attachment site
Structure domains: ACP-like

Ligands and Environments

1 bound ligand:
Ligand ZN 2 x ZN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE BM30A
Spacegroup: P63
Unit cell:
a: 63.36Å b: 63.36Å c: 37.049Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.205 0.205 0.252
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

13 review citations

The structural biology of type II fatty acid biosynthesis.
White et al. (2005)
12 more

8 mentions without citation

Non-homologous isofunctional enzymes: a systematic analysis of alternative solutions in enzyme evolution.
Omelchenko et al. (2010)
7 more