› 5vln

Solution NMR

NMR structure of the N-domain of troponin C bound to switch region of troponin I

Released:
DOI: 10.2210/pdb5vln/pdb
PDB entry 5vln coloured by chain, ensemble of 8 models, front view.
PDB entry 5vln coloured by chain, ensemble of 8 models, side view.
PDB entry 5vln coloured by chain, ensemble of 8 models, top view.
Source organism: Homo sapiens
Primary publication:
Structures reveal details of small molecule binding to cardiac troponin.
Cai F, Li MX, Pineda-Sanabria SE, Gelozia S, Lindert S, West F, Sykes BD, Hwang PM
J Mol Cell Cardiol 101 134-144 (2016)
PMID: 27825981

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-148572 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Troponin C, slow skeletal and cardiac muscles; Troponin I, cardiac muscle Chain: A
Molecule details ›
Chain: A
Length: 120 amino acids
Theoretical weight: 13.5 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P63316 (Residues: 1-92; Coverage: 57%)
  • Canonical: P19429 (Residues: 139-164; Coverage: 12%)
Gene names: TNNC, TNNC1, TNNI3
Sequence domains: EF-hand domain pair

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 91%
Refinement method: molecular dynamics
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Computational Studies of Cardiac and Skeletal Troponin.
Bowman et al. (2019)
1 more

1 mention without citation

X-ray structure of a human cardiac muscle troponin C/troponin I chimera in two crystal forms.
Yan et al. (2022)