› 3i5f

X-ray diffraction
3.1Å resolution

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-129199 (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
Myosin heavy chain isoform A Chain: A
Molecule details ›
Chain: A
Length: 839 amino acids
Theoretical weight: 95.94 KDa
UniProt:
  • Canonical: O44934 (Residues: 1-839; Coverage: 43%)
Sequence domains:
Myosin regulatory light chain LC-2, mantle muscle Chain: B
Molecule details ›
Chain: B
Length: 153 amino acids
Theoretical weight: 17.58 KDa
Source organism: Todarodes pacificus
UniProt:
  • Canonical: P08052 (Residues: 1-153; Coverage: 100%)
Sequence domains: EF-hand domain pair
Structure domains: EF-hand
Myosin catalytic light chain LC-1, mantle muscle Chain: C
Molecule details ›
Chain: C
Length: 159 amino acids
Theoretical weight: 18.08 KDa
Source organism: Todarodes pacificus
UniProt:
  • Canonical: P05945 (Residues: 2-160; Coverage: 99%)
Sequence domains: EF-hand domain
Structure domains: EF-hand

Ligands and Environments

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

Experiments and Validation Details

Entry percentile scores
X-ray source: CHESS BEAMLINE A1
Spacegroup: C2
Unit cell:
a: 187.415Å b: 101.687Å c: 94.751Å
α: 90° β: 119.75° γ: 90°
R-values:
R R work R free
0.244 0.244 0.317

Quick links

Citations

7 review citations

Structural and functional insights into the Myosin motor mechanism.
Sweeney et al. (2010)
6 more

15 mentions without citation

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