› 2q0u

X-ray diffraction
1.45Å resolution

Structure of Pectenotoxin-2 and Latrunculin B Bound to Actin

Released:
DOI: 10.2210/pdb2q0u/pdb
PDB entry 2q0u coloured by chain, front view.
PDB entry 2q0u coloured by chain, side view.
PDB entry 2q0u coloured by chain, top view.
Source organism: Oryctolagus cuniculus
Primary publication:
A structural basis for regulation of actin polymerization by pectenotoxins.
Allingham JS, Miles CO, Rayment I
J Mol Biol 371 959-70 (2007)
PMID: 17599353

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-159302 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Actin, alpha skeletal muscle Chain: A
Molecule details ›
Chain: A
Length: 375 amino acids
Theoretical weight: 41.88 KDa
Source organism: Oryctolagus cuniculus
UniProt:
  • Canonical: P68135 (Residues: 3-377; Coverage: 100%)
Gene names: ACTA, ACTA1
Sequence domains: Actin
Structure domains:

Ligands and Environments

4 bound ligands:
Ligand CA 2 x CA
Ligand ATP 1 x ATP
Ligand LAB 1 x LAB
Ligand PXT 1 x PXT
1 modified residue:
Ligand HIC 1 x HIC

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-BM
Spacegroup: C2
Unit cell:
a: 57.683Å b: 54.342Å c: 105.895Å
α: 90° β: 90.27° γ: 90°
R-values:
R R work R free
0.166 0.165 0.181

Quick links

Citations

13 review citations

Marine natural products.
Blunt et al. (2009)
12 more

7 mentions without citation

Actin structure and function.
Dominguez et al. (2011)
6 more