Research workbench
AlphaFold monomer V2.0 prediction for protein tic 214 (A0A393)
Analyse AlphaFold monomer V2.0 prediction for protein tic 214 (A0A393) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- A0A393
- Type
- protein
- Length
- 1,874 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x7a1388B6Aad67B04634A32f63b8A6D6005eab86c
- Molecule
- Protein tic 214
- UniProt
- A0A393
- Pockets
- 16 · best druggability 0.71
Structure
1 distinct chain · 39% helix, 3% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein tic 214 | protein | 1874 | 39% helix, 3% strand | A0A393 |
Pockets
16 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 118 | 0.71 | 0.92 | 23 | empty |
| 2 | 582 | 0.71 | 0.79 | 47 | empty |
| 3 | 440 | 0.63 | 0.77 | 44 | empty |
| 4 | 308 | 0.57 | 0.76 | 33 | empty |
| 5 | 198 | 0.55 | 0.79 | 22 | 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 A0A393
- Elsewhere: UniProt A0A393 · AlphaFold DB A0A393
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