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AlphaFold monomer V2.0 prediction for E3 ubiquitin-protein ligase NEDD4-like (Q5RBF2)
Analyse AlphaFold monomer V2.0 prediction for E3 ubiquitin-protein ligase NEDD4-like… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q5RBF2
- Type
- protein
- Length
- 959 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x23d54A6F00551fa0b7Dc770fB4753a25fEe18154
- Molecule
- E3 ubiquitin-protein ligase NEDD4-like
- UniProt
- Q5RBF2
- Pockets
- 6 · best druggability 0.70
Structure
1 distinct chain · 23% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | E3 ubiquitin-protein ligase NEDD4-like | protein | 959 | 23% helix, 18% strand | Q5RBF2 |
Pockets
6 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 428 | 0.70 | 0.81 | 50 | empty |
| 2 | 1127 | 0.70 | 0.74 | 106 | empty |
| 3 | 484 | 0.63 | 0.76 | 39 | empty |
| 4 | 101 | 0.36 | 0.74 | 17 | empty |
| 5 | 76 | 0.34 | 0.75 | 12 | 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 Q5RBF2
- Elsewhere: UniProt Q5RBF2 · AlphaFold DB Q5RBF2
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