› 1wku

X-ray diffraction
1.6Å resolution

High resolution structure of the human alpha-actinin isoform 3

Released:
DOI: 10.2210/pdb1wku/pdb
PDB entry 1wku coloured by chain, front view.
PDB entry 1wku coloured by chain, side view.
PDB entry 1wku coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
The crystal structure of the actin binding domain from alpha-actinin in its closed conformation: structural insight into phospholipid regulation of alpha-actinin.
Franzot G, Sjöblom B, Gautel M, Djinović Carugo K
J Mol Biol 348 151-65 (2005)
PMID: 15808860

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-170589 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Alpha-actinin-3 Chains: A, B
Molecule details ›
Chains: A, B
Length: 254 amino acids
Theoretical weight: 29.28 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q08043 (Residues: 26-273; Coverage: 28%)
Gene name: ACTN3
Sequence domains: Calponin homology (CH) domain
Structure domains: Calponin-like domain

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ELETTRA BEAMLINE 5.2R
Spacegroup: P1
Unit cell:
a: 38.499Å b: 45.96Å c: 66.998Å
α: 86.67° β: 87.8° γ: 87.33°
R-values:
R R work R free
0.182 0.182 0.208
Expression system: Escherichia coli

Quick links

Citations

14 review citations

Filamins: promiscuous organizers of the cytoskeleton.
Popowicz et al. (2006)
13 more

10 mentions without citation

The structure and regulation of human muscle α-actinin.
Ribeiro Ede et al. (2014)
9 more