› 6djn

Electron Microscopy
3.1Å resolution

Cryo-EM structure of ADP-Pi-actin filaments

Released:
DOI: 10.2210/pdb6djn/pdb
PDB entry 6djn coloured by chain, front view.
PDB entry 6djn coloured by chain, side view.
PDB entry 6djn coloured by chain, top view.
Source organism: Gallus gallus
Primary publication:
Mechanism of actin polymerization revealed by cryo-EM structures of actin filaments with three different bound nucleotides.
Chou SZ, Pollard TD
Proc Natl Acad Sci U S A 116 4265-4274 (2019)
PMID: 30760599
Related structures: EMD-7937

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-159348 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Actin, alpha skeletal muscle Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 375 amino acids
Theoretical weight: 41.88 KDa
Source organism: Gallus gallus
UniProt:
  • Canonical: P68139 (Residues: 3-377; Coverage: 100%)
Gene names: ACTA, ACTA1
Sequence domains: Actin
Structure domains:

Ligands and Environments

3 bound ligands:
Ligand MG 4 x MG
Ligand ADP 4 x ADP
Ligand PO4 4 x PO4
1 modified residue:
Ligand HIC 4 x HIC

Experiments and Validation Details

Entry percentile scores
Resolution: 3.1Å
Relevant EMDB volumes: EMD-7937

Quick links

Citations

13 review citations

Enzymatic Noncovalent Synthesis.
He et al. (2020)
12 more

13 mentions without citation

Lysine acetylation of cytoskeletal proteins: Emergence of an actin code.
A et al. (2020)
12 more