› 2q36

X-ray diffraction
2.5Å resolution

Actin Dimer Cross-linked between Residues 191 and 374 and complexed with Kabiramide C

Released:
DOI: 10.2210/pdb2q36/pdb
PDB entry 2q36 coloured by chain, front view.
PDB entry 2q36 coloured by chain, side view.
PDB entry 2q36 coloured by chain, top view.
Source organism: Oryctolagus cuniculus
Primary publication:
Multiple crystal structures of actin dimers and their implications for interactions in the actin filament.
Sawaya MR, Kudryashov DS, Pashkov I, Adisetiyo H, Reisler E, Yeates TO
Acta Crystallogr D Biol Crystallogr 64 454-65 (2008)
PMID: 18391412

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-159317 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Actin, alpha skeletal muscle Chain: A
Molecule details ›
Chain: A
Length: 375 amino acids
Theoretical weight: 41.86 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 1 x CA
Ligand SO4 2 x SO4
Ligand ATP 1 x ATP
Ligand KAB 1 x KAB
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 8.2.2
Spacegroup: P212121
Unit cell:
a: 40.539Å b: 74.276Å c: 144.474Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.177 0.175 0.223

Quick links

Citations

3 review citations

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

98 mentions without citation

Clinical, genetic and imaging findings identify new causes for corpus callosum development syndromes.
Edwards et al. (2014)
97 more