Research workbench
NMR structure of the MG2+-loaded C terminal domain of cardiac troponin C bound to the N terminal domain of cardiac troponin I
Analyse NMR structure of the MG2+-loaded C terminal domain of cardiac troponin C bound… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1SBJ
- Type
- protein
- Length
- 81 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Troponin C, slow skeletal and cardiac muscles
- UniProt
- P09860
- Ligands
- MG
Structure
solution nmr · 1 distinct chain · 47% helix, 2% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Troponin C, slow skeletal and cardiac muscles | protein | 81 | 47% helix, 2% strand | P09860 |
Ligands and binding sites
- MG · Magnesium ion · metal · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 1SBJ · NMR Structure of the Mg2+-loaded C Terminal Domain of Cardiac Troponin C Bound to the N… · the same entry in another collection · chain A against A, TM-score 1.00
- P09860 · AlphaFold monomer V2.0 prediction for troponin C, slow skeletal and cardiac muscles… · a predicted model of the same protein · chain A against A, TM-score 0.73
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt P09860
- Elsewhere: RCSB PDB 1SBJ · PDBe 1SBJ · UniProt P09860
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