› 2q31

X-ray diffraction
2.7Å resolution

Actin Dimer Cross-linked Between Residues 41 and 374 and proteolytically cleaved by subtilisin between residues 47 and 48.

Released:
DOI: 10.2210/pdb2q31/pdb
PDB entry 2q31 coloured by chain, front view.
PDB entry 2q31 coloured by chain, side view.
PDB entry 2q31 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
OpenAccess logo 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 Chains: A, B
Molecule details ›
Chains: A, B
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

3 bound ligands:
Ligand CA 2 x CA
Ligand ATP 2 x ATP
Ligand LAR 2 x LAR
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 8.2.2
Spacegroup: P21
Unit cell:
a: 108.253Å b: 71.984Å c: 54.703Å
α: 90° β: 104.68° γ: 90°
R-values:
R R work R free
0.251 0.249 0.288

Quick links

Citations

3 review citations

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

171 mentions without citation

The integrins.
Takada et al. (2007)
170 more