Research workbench
AlphaFold monomer V2.0 prediction for E3 ubiquitin-protein ligase TRIM39 (Q1XHU0)
Analyse AlphaFold monomer V2.0 prediction for E3 ubiquitin-protein ligase TRIM39… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q1XHU0
- Type
- protein
- Length
- 518 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x5881B09f2D8e743400698633641fc1cD2Ed2BE6F
- Molecule
- E3 ubiquitin-protein ligase TRIM39
- UniProt
- Q1XHU0
- Pockets
- 4 · best druggability 0.58
Structure
1 distinct chain · 42% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | E3 ubiquitin-protein ligase TRIM39 | protein | 518 | 42% helix, 19% strand | Q1XHU0 |
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 390 | 0.58 | 0.75 | 34 | empty |
| 2 | 181 | 0.51 | 0.77 | 24 | empty |
| 3 | 71 | 0.39 | 0.78 | 13 | empty |
| 4 | 88 | 0.38 | 0.76 | 19 | 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 Q1XHU0
- Elsewhere: UniProt Q1XHU0 · AlphaFold DB Q1XHU0
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