Research workbench
AlphaFold monomer V2.0 prediction for restriction of telomere capping protein 5 (A7TNS4)
Analyse AlphaFold monomer V2.0 prediction for restriction of telomere capping protein 5… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- A7TNS4
- Type
- protein
- Length
- 562 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x1B6204b594D54D3E83B7C102EA0B596aAf1188e4
- Molecule
- Restriction of telomere capping protein 5
- UniProt
- A7TNS4
- Pockets
- 8 · best druggability 0.74
Structure
1 distinct chain · 43% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Restriction of telomere capping protein 5 | protein | 562 | 43% helix, 16% strand | A7TNS4 |
Pockets
8 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 519 | 0.74 | 0.82 | 50 | empty |
| 2 | 151 | 0.48 | 0.77 | 30 | empty |
| 3 | 125 | 0.46 | 0.78 | 25 | empty |
| 4 | 120 | 0.39 | 0.75 | 19 | empty |
| 5 | 54 | 0.38 | 0.80 | 15 | 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 A7TNS4
- Elsewhere: UniProt A7TNS4 · AlphaFold DB A7TNS4
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