› 1b7t

X-ray diffraction
2.5Å resolution

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-139482 (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
Myosin heavy chain, striated muscle Chain: A
Molecule details ›
Chain: A
Length: 835 amino acids
Theoretical weight: 95.32 KDa
Source organism: Argopecten irradians
UniProt:
  • Canonical: P24733 (Residues: 1-835; Coverage: 43%)
Sequence domains:
Structure domains:
Myosin regulatory light chain, striated adductor muscle Chain: Y
Molecule details ›
Chain: Y
Length: 156 amino acids
Theoretical weight: 17.56 KDa
Source organism: Argopecten irradians
UniProt:
  • Canonical: P13543 (Residues: 2-157; Coverage: 99%)
Sequence domains: EF-hand domain pair
Structure domains: EF-hand
Myosin essential light chain, striated adductor muscle Chain: Z
Molecule details ›
Chain: Z
Length: 156 amino acids
Theoretical weight: 17.64 KDa
Source organism: Argopecten irradians
UniProt:
  • Canonical: P07291 (Residues: 2-157; Coverage: 99%)
Sequence domains: EF-hand domain pair
Structure domains: EF-hand

Ligands and Environments

3 bound ligands:
Ligand MG 2 x MG
Ligand ADP 1 x ADP
Ligand CA 1 x CA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: CHESS BEAMLINE F1
Spacegroup: P1
Unit cell:
a: 51.7Å b: 58.9Å c: 138.9Å
α: 89.1° β: 90° γ: 73.5°
R-values:
R R work R free
0.224 0.224 0.297

Quick links

Citations

36 review citations

Intrinsically disordered protein.
Dunker et al. (2001)
35 more

19 mentions without citation

Three perspectives on the molecular basis of hypercontractility caused by hypertrophic cardiomyopathy mutations.
Spudich JA. (2019)
18 more