Research workbench
AlphaFold monomer V2.0 prediction for E3 ubiquitin-protein ligase NEURL3 (Q96EH8)
Analyse AlphaFold monomer V2.0 prediction for E3 ubiquitin-protein ligase NEURL3… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q96EH8
- Type
- protein
- Length
- 262 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x5Ed6BFcdacb6badB27582f1166F4aAdB839FC5D7
- Molecule
- E3 ubiquitin-protein ligase NEURL3
- UniProt
- Q96EH8
- Pockets
- 2 · best druggability 0.49
Structure
1 distinct chain · 9% helix, 32% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | E3 ubiquitin-protein ligase NEURL3 | protein | 262 | 9% helix, 32% strand | Q96EH8 |
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 212 | 0.49 | 0.75 | 25 | empty |
| 2 | 70 | 0.29 | 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 Q96EH8
- Elsewhere: UniProt Q96EH8 · AlphaFold DB Q96EH8
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