› 2mq0

Solution NMR

NMR structure of the c3 domain of human cardiac myosin binding protein-c

Released:
DOI: 10.2210/pdb2mq0/pdb
PDB entry 2mq0 coloured by chain, ensemble of 10 models, front view.
PDB entry 2mq0 coloured by chain, ensemble of 10 models, side view.
PDB entry 2mq0 coloured by chain, ensemble of 10 models, top view.
Source organism: Homo sapiens
Primary publication:
Structural characterization of the C3 domain of cardiac myosin binding protein C and its hypertrophic cardiomyopathy-related R502W mutant.
Zhang XL, De S, McIntosh LP, Paetzel M
Biochemistry 53 5332-42 (2014)
PMID: 25058872

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-556549 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Myosin-binding protein C, cardiac-type Chain: A
Molecule details ›
Chain: A
Length: 95 amino acids
Theoretical weight: 10.83 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q14896 (Residues: 453-543; 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
Chemical shift assignment: 92%
Refinement method: torsion angle dynamics
Expression system: Escherichia coli

Quick links

Citations

2 review citations

The Role of Cardiac Myosin Binding Protein C3 in Hypertrophic Cardiomyopathy-Progress and Novel Therapeutic Opportunities.
Mohamed et al. (2017)
1 more

5 mentions without citation

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