Research workbench
AlphaFold monomer V2.0 prediction for restriction of telomere capping protein 1 (A7TR10)
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
- A7TR10
- Type
- protein
- Length
- 1,313 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x866b846BF04951b9214b46ED5E3FC54E8e4ab00f
- Molecule
- Restriction of telomere capping protein 1
- UniProt
- A7TR10
- Pockets
- 9 · best druggability 0.78
Structure
1 distinct chain · 17% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Restriction of telomere capping protein 1 | protein | 1313 | 17% helix, 15% strand | A7TR10 |
Pockets
9 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 350 | 0.78 | 0.88 | 35 | empty |
| 2 | 1051 | 0.74 | 0.77 | 71 | empty |
| 3 | 677 | 0.68 | 0.76 | 74 | empty |
| 4 | 282 | 0.60 | 0.79 | 35 | empty |
| 5 | 303 | 0.59 | 0.77 | 32 | 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 A7TR10
- Elsewhere: UniProt A7TR10 · AlphaFold DB A7TR10
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.