Research workbench
NMR structure of the N-domain of troponin C bound to the switch region of troponin I and the covalent levosimendan analog I9
Analyse NMR structure of the N-domain of troponin C bound to the switch region of… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2N7L
- Type
- protein
- Length
- 140 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Troponin C/TROPONIN I chimera
- UniProt
- P63316, P19429
- Ligands
- CA
- Pockets
- 3 · best druggability 0.67
Structure
solution nmr · 1 distinct chain · 52% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| C | Troponin C/TROPONIN I chimera | protein | 140 | 52% helix, 0% strand | P63316, P19429 |
Ligands and binding sites
- CA · Calcium ion · metal · chains C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 189 | 0.67 | 0.85 | 33 | empty |
| 2 | 84 | 0.37 | 0.76 | 11 | empty |
| 3 | 59 | 0.33 | 0.76 | 10 | empty |
Modifications
Observed in the structure: 1 modified (nonstandard).
Compared structures
- 2N7L · NMR structure of the N-domain of troponin C bound to the switch region of troponin I and… · the same entry in another collection · chain C against C, TM-score 1.00
- P63316 · AlphaFold monomer V2.0 prediction for troponin C, slow skeletal and cardiac muscles… · a predicted model of the same protein · chain C against A, TM-score 0.51
- P19429 · AlphaFold monomer V2.0 prediction for troponin I, cardiac muscle (P19429) · a predicted model of the same protein · chain C against A, TM-score 0.21
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 P63316
- Every structure of UniProt P19429
- Elsewhere: RCSB PDB 2N7L · PDBe 2N7L · UniProt P63316 · UniProt P19429
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