MolNFT v1 · #138238 · protein
NMR structure of the N-domain of troponin C bound to switch region of troponin I and 3-methyldiphenylamine (solvent exposed mode)
5WCL · Troponin C, slow skeletal and cardiac MUSCLES,TROPONIN I…: “NMR structure of the N-domain of troponin C bound to switch region of troponin I and 3-methyldiphenylamine…”. Solution nmr, 1 ligand (9XG), 1 pocket (best druggability…
- PDB
- 5WCL
- Type
- protein
- Length
- 120 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
- 9XG
- Pockets
- 1 · best druggability 0.69
Structure
solution nmr · 1 distinct chain · 54% helix, 2% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Troponin C, slow skeletal and cardiac MUSCLES,TROPONIN I, cardiac muscle | protein | 120 | 54% helix, 2% strand | P63316, P19429 |
Ligands and binding sites
- 9XG · 3-methyl-N-phenylaniline · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 150 | 0.69 | 0.89 | 31 | 9XG |
Compared structures
- 5WCL · NMR structure of the N-domain of troponin C bound to switch region of troponin I and… · 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 0.69
- 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 0.24
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 5WCL · PDBe 5WCL · UniProt P63316 · UniProt P19429
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