MolNFT v1 · #188838 · protein
NMR structure of the cntnc-ctni chimera bound to W6
7UHA · Troponin C, slow skeletal and cardiac MUSCLES,TROPONIN I…: “NMR structure of the cntnc-ctni chimera bound to W6”. Solution nmr, 2 ligands (WW6, CA), 2 pockets (best druggability 0.68). MolNFT v1 #188838 on GenesisL1: 3D structure…
- PDB
- 7UHA
- Type
- protein
- Length
- 125 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
- WW6, CA
- Pockets
- 2 · best druggability 0.68
Structure
solution nmr · 1 distinct chain · 58% helix, 2% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Troponin C, slow skeletal and cardiac MUSCLES,TROPONIN I, cardiac muscle | protein | 125 | 58% helix, 2% strand | P63316, P19429 |
Ligands and binding sites
- WW6 · N-(5-aminopentyl)-5-chloronaphthalene-1-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, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 288 | 0.68 | 0.83 | 35 | WW6 |
| 2 | 145 | 0.43 | 0.75 | 25 | empty |
Compared structures
- 7UHA · NMR structure of the cNTnC-cTnI chimera bound to W6 · 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 0.64
- 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 0.25
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 7UHA · PDBe 7UHA · UniProt P63316 · UniProt P19429
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