X-ray diffraction
3.1Å resolution

Function and Biology Details

Structure analysis Details

Assembly composition:
hetero tetramer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Actin, alpha skeletal muscle Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 377 amino acids
Theoretical weight: 42.1 KDa
Source organism: Oryctolagus cuniculus
Expression system: Escherichia coli BL21
  • Canonical: P68135 (Residues: 1-377; Coverage: 100%)
Gene names: ACTA, ACTA1
Sequence domains: Actin
Structure domains:
Myocardin-related transcription factor A Chain: M
Molecule details ›
Chain: M
Length: 137 amino acids
Theoretical weight: 15.78 KDa
Source organism: Mus musculus
Expression system: Escherichia coli BL21
  • Canonical: Q8K4J6 (Residues: 16-142; Coverage: 13%)
  • Best match: Q8K4J6-2 (Residues: 1-107)
Gene names: Bsac, Mal, Mkl1, Mrtfa
Sequence domains: RPEL repeat
Structure domains: Helix Hairpins

Ligands and Environments

3 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-2
Spacegroup: P43212
Unit cell:
a: 90.935Å b: 90.935Å c: 321.613Å
α: 90° β: 90° γ: 90°
R R work R free
0.237 0.235 0.28
Expression system: Escherichia coli BL21