› 1pd6

Solution NMR

The NMR structure of domain C2 of human cardiac Myosin Binding Protein C

Released:
DOI: 10.2210/pdb1pd6/pdb
PDB entry 1pd6 coloured by chain, ensemble of 28 models, front view.
PDB entry 1pd6 coloured by chain, ensemble of 28 models, side view.
PDB entry 1pd6 coloured by chain, ensemble of 28 models, top view.
Source organism: Homo sapiens
Primary publication:
Dissecting the N-terminal myosin binding site of human cardiac myosin-binding protein C. Structure and myosin binding of domain C2.
Ababou A, Gautel M, Pfuhl M
J Biol Chem 282 9204-15 (2007)
PMID: 17192269

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: 104 amino acids
Theoretical weight: 11.77 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q14896 (Residues: 358-451; Coverage: 7%)
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
Refinement method: we have used ARIA protocols
Expression system: Escherichia coli

Quick links

Citations

16 review citations

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

5 mentions without citation

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