› 2y83

Electron Microscopy
22.9Å resolution

Actin filament pointed end

Released:
DOI: 10.2210/pdb2y83/pdb
PDB entry 2y83 coloured by chain, front view.
PDB entry 2y83 coloured by chain, side view.
PDB entry 2y83 coloured by chain, top view.
Source organism: Oryctolagus cuniculus
Primary publication:
Structural basis for the slow dynamics of the actin filament pointed end.
Narita A, Oda T, Maéda Y
EMBO J 30 1230-7 (2011)
PMID: 21378753
Related structures: EMD-1872

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo hexamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-159336 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Actin, alpha skeletal muscle Chains: O, P, Q, R, S, T
Molecule details ›
Chains: O, P, Q, R, S, T
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

Ligands and Environments

2 bound ligands:
Ligand ADP 6 x ADP
Ligand CA 6 x CA
No modified residues

Experiments and Validation Details

Entry percentile scores
Resolution: 22.9Å
Relevant EMDB volumes: EMD-1872

Quick links

Citations

4 review citations

Towards a structural understanding of the remodeling of the actin cytoskeleton.
Merino et al. (2020)
3 more

5 mentions without citation

Polymerization and depolymerization of actin with nucleotide states at filament ends.
Fujiwara et al. (2018)
4 more