› 1scm

X-ray diffraction
2.8Å resolution

STRUCTURE OF THE REGULATORY DOMAIN OF SCALLOP MYOSIN AT 2.8 ANGSTROMS RESOLUTION

Released:
DOI: 10.2210/pdb1scm/pdb
PDB entry 1scm coloured by chain, front view.
PDB entry 1scm coloured by chain, side view.
PDB entry 1scm coloured by chain, top view.
Source organism: Argopecten irradians
Primary publication:
Structure of the regulatory domain of scallop myosin at 2.8 A resolution.
Xie X, Harrison DH, Schlichting I, Sweet RM, Kalabokis VN, Szent-Györgyi AG, Cohen C
Nature 368 306-12 (1994)
PMID: 8127365

Function and Biology Details

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

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: 60 amino acids
Theoretical weight: 7.48 KDa
Source organism: Argopecten irradians
Expression system: Not provided
UniProt:
  • Canonical: P24733 (Residues: 777-836; Coverage: 3%)
Structure domains: Myosin, subunit A
Myosin regulatory light chain, striated adductor muscle Chain: B
Molecule details ›
Chain: B
Length: 145 amino acids
Theoretical weight: 16.52 KDa
Source organism: Argopecten irradians
Expression system: Not provided
UniProt:
  • Canonical: P13543 (Residues: 13-157; Coverage: 92%)
Sequence domains: EF-hand domain pair
Structure domains: EF-hand
Myosin essential light chain, striated adductor muscle Chain: C
Molecule details ›
Chain: C
Length: 149 amino acids
Theoretical weight: 16.79 KDa
Source organism: Argopecten irradians
Expression system: Not provided
UniProt:
  • Canonical: P07291 (Residues: 5-153; Coverage: 95%)
Sequence domains: EF-hand domain pair
Structure domains: EF-hand

Ligands and Environments

1 bound ligand:
Ligand CA 2 x CA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS
Spacegroup: P21
Unit cell:
a: 52.5Å b: 87Å c: 55.5Å
α: 90° β: 114.5° γ: 90°
R-values:
R R work R free
0.201 0.201 not available
Expression system: Not provided

Quick links

Citations

42 review citations

Regulation of contraction in striated muscle.
Gordon et al. (2000)
41 more

6 mentions without citation

Overview of protein structural and functional folds.
Sun et al. (2004)
5 more