Research workbench
AlphaFold monomer V2.0 prediction for E3 ubiquitin-protein ligase RNF123 (Q5XPI3)
Analyse AlphaFold monomer V2.0 prediction for E3 ubiquitin-protein ligase RNF123… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q5XPI3
- Type
- protein
- Length
- 1,314 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xd10960F956646DE8b64d3598984c91C2d5Af3D7b
- Molecule
- E3 ubiquitin-protein ligase RNF123
- UniProt
- Q5XPI3
- Pockets
- 17 · best druggability 0.84
Structure
1 distinct chain · 50% helix, 9% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | E3 ubiquitin-protein ligase RNF123 | protein | 1314 | 50% helix, 9% strand | Q5XPI3 |
Pockets
17 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1015 | 0.84 | 0.85 | 107 | empty |
| 2 | 1112 | 0.79 | 0.80 | 89 | empty |
| 3 | 950 | 0.76 | 0.79 | 91 | empty |
| 4 | 97 | 0.56 | 0.85 | 22 | empty |
| 5 | 195 | 0.55 | 0.79 | 29 | 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 Q5XPI3
- Elsewhere: UniProt Q5XPI3 · AlphaFold DB Q5XPI3
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