Research workbench
AlphaFold monomer V2.0 prediction for E3 ubiquitin-protein ligase TRIM47 (Q96LD4)
Analyse AlphaFold monomer V2.0 prediction for E3 ubiquitin-protein ligase TRIM47… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q96LD4
- Type
- protein
- Length
- 638 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xf54df32EdA57e78399A3CCeF3883225956Cb8837
- Molecule
- E3 ubiquitin-protein ligase TRIM47
- UniProt
- Q96LD4
- Pockets
- 4 · best druggability 0.41
Structure
1 distinct chain · 34% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | E3 ubiquitin-protein ligase TRIM47 | protein | 638 | 34% helix, 18% strand | Q96LD4 |
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 | 156 | 0.41 | 0.73 | 28 | empty |
| 2 | 50 | 0.38 | 0.80 | 13 | empty |
| 3 | 108 | 0.35 | 0.73 | 15 | empty |
| 4 | 84 | 0.31 | 0.73 | 20 | 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 Q96LD4
- Elsewhere: UniProt Q96LD4 · AlphaFold DB Q96LD4
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