› 2avg

Solution NMR

NMR structure of cC1 domain from Human Cardiac Myosin Binding Protein C

Released:
DOI: 10.2210/pdb2avg/pdb
PDB entry 2avg coloured by chain, ensemble of 29 models, front view.
PDB entry 2avg coloured by chain, ensemble of 29 models, side view.
PDB entry 2avg coloured by chain, ensemble of 29 models, top view.
Source organism: Homo sapiens
Primary publication:
Myosin binding protein C positioned to play a key role in regulation of muscle contraction: structure and interactions of domain C1.
Ababou A, Rostkova E, Mistry S, Le Masurier C, Gautel M, Pfuhl M
J Mol Biol 384 615-30 (2008)
PMID: 18926831

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-172117 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Myosin-binding protein C, cardiac-type Chain: A
Molecule details ›
Chain: A
Length: 120 amino acids
Theoretical weight: 13.49 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q14896 (Residues: 151-260; Coverage: 9%)
Gene name: MYBPC3
Sequence domains: Immunoglobulin I-set domain
Structure domains: Immunoglobulins

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 79%
Refinement method: simulated annealing using ARIA program
Expression system: Escherichia coli

Quick links

Citations

18 review citations

In the thick of it: HCM-causing mutations in myosin binding proteins of the thick filament.
Harris et al. (2011)
17 more

7 mentions without citation

The myosin mesa and the basis of hypercontractility caused by hypertrophic cardiomyopathy mutations.
Nag et al. (2017)
6 more