Research workbench
AlphaFold monomer V2.0 prediction for E3 ubiquitin-protein ligase XBAT33 (Q4FE45)
Analyse AlphaFold monomer V2.0 prediction for E3 ubiquitin-protein ligase XBAT33… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q4FE45
- Type
- protein
- Length
- 513 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xBF0D2e107Ce1EcD2C4369B042274201DB719AaAF
- Molecule
- E3 ubiquitin-protein ligase XBAT33
- UniProt
- Q4FE45
- Pockets
- 3 · best druggability 0.67
Structure
1 distinct chain · 35% helix, 3% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | E3 ubiquitin-protein ligase XBAT33 | protein | 513 | 35% helix, 3% strand | Q4FE45 |
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 573 | 0.67 | 0.77 | 57 | empty |
| 2 | 288 | 0.56 | 0.76 | 36 | empty |
| 3 | 97 | 0.35 | 0.74 | 16 | empty |
Modifications
Observed in the structure: 1 disulfide (disulfide).
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 Q4FE45
- Elsewhere: UniProt Q4FE45 · AlphaFold DB Q4FE45
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