Research workbench
AlphaFold monomer V2.0 prediction for E3 ubiquitin-protein ligase RNF138 (Q1L721)
Analyse AlphaFold monomer V2.0 prediction for E3 ubiquitin-protein ligase RNF138… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q1L721
- Type
- protein
- Length
- 222 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x9d7467021Db73aeAa95A2Ab5150B26f506bE6044
- Molecule
- E3 ubiquitin-protein ligase RNF138
- UniProt
- Q1L721
- Pockets
- 3 · best druggability 0.49
Structure
1 distinct chain · 37% helix, 11% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | E3 ubiquitin-protein ligase RNF138 | protein | 222 | 37% helix, 11% strand | Q1L721 |
Pockets
3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 108 | 0.49 | 0.81 | 18 | empty |
| 2 | 162 | 0.46 | 0.76 | 27 | empty |
| 3 | 142 | 0.40 | 0.74 | 24 | 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 Q1L721
- Elsewhere: UniProt Q1L721 · AlphaFold DB Q1L721
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