Research workbench
AlphaFold monomer V2.0 prediction for restriction of telomere capping protein 1 (C4YN69)
Analyse AlphaFold monomer V2.0 prediction for restriction of telomere capping protein 1… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- C4YN69
- Type
- protein
- Length
- 1,088 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xfD2aa30896c43ba48ACc736586610789048c2c7a
- Molecule
- Restriction of telomere capping protein 1
- UniProt
- C4YN69
- Pockets
- 8 · best druggability 0.79
Structure
1 distinct chain · 16% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Restriction of telomere capping protein 1 | protein | 1088 | 16% helix, 18% strand | C4YN69 |
Pockets
8 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 941 | 0.79 | 0.81 | 70 | empty |
| 2 | 191 | 0.57 | 0.80 | 25 | empty |
| 3 | 241 | 0.50 | 0.75 | 32 | empty |
| 4 | 236 | 0.49 | 0.75 | 31 | empty |
| 5 | 58 | 0.47 | 0.85 | 17 | empty |
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 C4YN69
- Elsewhere: UniProt C4YN69 · AlphaFold DB C4YN69
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