Research workbench
AlphaFold monomer V2.0 prediction for E3 ubiquitin-protein ligase TRIM11 (Q99PQ2)
Analyse AlphaFold monomer V2.0 prediction for E3 ubiquitin-protein ligase TRIM11… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q99PQ2
- Type
- protein
- Length
- 467 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x0EA189b2343A464f560b44103f6A3396Da1dA8a9
- Molecule
- E3 ubiquitin-protein ligase TRIM11
- UniProt
- Q99PQ2
- Pockets
- 4 · best druggability 0.47
Structure
1 distinct chain · 36% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | E3 ubiquitin-protein ligase TRIM11 | protein | 467 | 36% helix, 20% strand | Q99PQ2 |
Pockets
4 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 111 | 0.47 | 0.79 | 25 | empty |
| 2 | 110 | 0.43 | 0.77 | 28 | empty |
| 3 | 64 | 0.30 | 0.74 | 12 | empty |
| 4 | 56 | 0.28 | 0.74 | 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 Q99PQ2
- Elsewhere: UniProt Q99PQ2 · AlphaFold DB Q99PQ2
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