Research workbench
AlphaFold monomer V2.0 prediction for restriction of telomere capping protein 1 (A3GIA4)
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
- A3GIA4
- Type
- protein
- Length
- 1,105 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x5BeA89782341f98147F2D811B063F91F0aE7D7bF
- Molecule
- Restriction of telomere capping protein 1
- UniProt
- A3GIA4
- Pockets
- 6 · best druggability 0.80
Structure
1 distinct chain · 16% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Restriction of telomere capping protein 1 | protein | 1105 | 16% helix, 18% strand | A3GIA4 |
Pockets
6 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 783 | 0.80 | 0.83 | 58 | empty |
| 2 | 390 | 0.63 | 0.78 | 39 | empty |
| 3 | 434 | 0.63 | 0.77 | 58 | empty |
| 4 | 156 | 0.49 | 0.78 | 22 | empty |
| 5 | 120 | 0.48 | 0.79 | 14 | 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 A3GIA4
- Elsewhere: UniProt A3GIA4 · AlphaFold DB A3GIA4
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