Research workbench
AlphaFold monomer V2.0 prediction for acetyltransferase TRI7 (Q9C1B8)
Analyse AlphaFold monomer V2.0 prediction for acetyltransferase TRI7 (Q9C1B8) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q9C1B8
- Type
- protein
- Length
- 441 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x4d07E6a23DeB6B95bd9b90EcB67368b7e8D3B77e
- Molecule
- Acetyltransferase TRI7
- UniProt
- Q9C1B8
- Pockets
- 7 · best druggability 0.86
Structure
1 distinct chain · 71% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Acetyltransferase TRI7 | protein | 441 | 71% helix, 0% strand | Q9C1B8 |
Pockets
7 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 958 | 0.86 | 0.87 | 83 | empty |
| 2 | 687 | 0.70 | 0.77 | 60 | empty |
| 3 | 292 | 0.66 | 0.82 | 31 | empty |
| 4 | 138 | 0.65 | 0.87 | 24 | empty |
| 5 | 103 | 0.64 | 0.89 | 27 | 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 Q9C1B8
- Elsewhere: UniProt Q9C1B8 · AlphaFold DB Q9C1B8
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