› 1kwo

X-ray diffraction
3.8Å resolution

SCALLOP MYOSIN S1-ATPgammaS-p-PDM IN THE ACTIN-DETACHED CONFORMATION

Released:
DOI: 10.2210/pdb1kwo/pdb
PDB entry 1kwo coloured by chain, front view.
PDB entry 1kwo coloured by chain, side view.
PDB entry 1kwo 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

4 bound ligands:
Ligand MG 2 x MG
Ligand AGS 1 x AGS
Ligand PDM 1 x PDM
Ligand CA 1 x CA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X12C
Spacegroup: P1
Unit cell:
a: 51.816Å b: 57.028Å c: 151.708Å
α: 95.16° β: 96.45° γ: 100.93°
R-values:
R R work R free
0.242 0.238 0.328

Quick links

Citations

7 review citations

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

7 mentions without citation

Mechanism of aromatic amino acid hydroxylation.
Fitzpatrick PF. (2003)
6 more