› 1kqm

X-ray diffraction
3Å resolution

SCALLOP MYOSIN S1-AMPPNP IN THE ACTIN-DETACHED CONFORMATION

Released:
DOI: 10.2210/pdb1kqm/pdb
PDB entry 1kqm coloured by chain, front view.
PDB entry 1kqm coloured by chain, side view.
PDB entry 1kqm coloured by chain, top view.
Source organism: Argopecten irradians
Primary publication:
Crystallographic findings on the internally uncoupled and near-rigor states of myosin: further insights into the mechanics of the motor.
Himmel DM, Gourinath S, Reshetnikova L, Shen Y, Szent-Györgyi AG, Cohen C
Proc Natl Acad Sci U S A 99 12645-50 (2002)
PMID: 12297624

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:
Myosin regulatory light chain, striated adductor muscle Chain: B
Molecule details ›
Chain: B
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: C
Molecule details ›
Chain: C
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 ANP 1 x ANP
Ligand CA 1 x CA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X26C
Spacegroup: P1
Unit cell:
a: 52.396Å b: 58.642Å c: 148.873Å
α: 81.64° β: 82.39° γ: 87.43°
R-values:
R R work R free
0.298 0.277 0.316

Quick links

Citations

6 review citations

SH3 domains: modules of protein-protein interactions.
Kurochkina et al. (2013)
5 more

6 mentions without citation

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