› 1hci

X-ray diffraction
2.8Å resolution

CRYSTAL STRUCTURE OF THE ROD DOMAIN OF ALPHA-ACTININ

Released:
DOI: 10.2210/pdb1hci/pdb
PDB entry 1hci coloured by chain, front view.
PDB entry 1hci coloured by chain, side view.
PDB entry 1hci coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Crystal structure of the alpha-actinin rod reveals an extensive torsional twist.
Ylänne J, Scheffzek K, Young P, Saraste M
Structure 9 597-604 (2001)
PMID: 11470434

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-152961 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Alpha-actinin-2 Chains: A, B
Molecule details ›
Chains: A, B
Length: 476 amino acids
Theoretical weight: 56.21 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P35609 (Residues: 274-746; Coverage: 53%)
Gene name: ACTN2
Sequence domains: Spectrin repeat
Structure domains: Methane Monooxygenase Hydroxylase; Chain G, domain 1

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-2
Spacegroup: P31
Unit cell:
a: 103.28Å b: 103.28Å c: 218.64Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.27 0.27 0.295
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

17 review citations

The structure and regulation of vinculin.
Ziegler et al. (2006)
16 more

19 mentions without citation

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