Research workbench
NMR structure of ctnc-tni chimera bound to calcium and A2
Analyse NMR structure of ctnc-tni chimera bound to calcium and A2 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7SVC
- Type
- protein
- Length
- 129 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Troponin C, slow skeletal and cardiac MUSCLES,TROPONIN I, cardiac muscle
- UniProt
- P63316, P19429
- Ligands
- C9W, CA
- Pockets
- 2 · best druggability 0.70
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,TROPONIN I, cardiac muscle | protein | 129 | 47% helix, 2% strand | P63316, P19429 |
Ligands and binding sites
- C9W · 4-(3-cyano-3-methylazetidine-1-carbonyl)-N-[(3R,4S)-7-fluoro-4-hydroxy-6-methyl-3,4-dihydro-2H-1-benzopyran-3-yl]-5-methyl-1H-pyrrole-2-sulfonamide · ligand · chains A
- CA · Calcium ion · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 225 | 0.70 | 0.86 | 31 | C9W |
| 2 | 394 | 0.63 | 0.77 | 45 | empty |
Compared structures
- 7SVC · NMR structure of cTnC-TnI chimera bound to calcium and A2 · the same entry in another collection · chain A against A, 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 A against A, TM-score 0.63
- P19429 · AlphaFold monomer V2.0 prediction for troponin I, cardiac muscle (P19429) · a predicted model of the same protein · chain A against A, TM-score 0.22
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 7SVC · PDBe 7SVC · UniProt P63316 · UniProt P19429
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