Research workbench
AlphaFold monomer V2.0 prediction for E3 ubiquitin-protein ligase RNF130 (Q8VEM1)
Analyse AlphaFold monomer V2.0 prediction for E3 ubiquitin-protein ligase RNF130… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q8VEM1
- Type
- protein
- Length
- 419 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xf33131c0E4A1330B6dE251178dC23570A939f9BD
- Molecule
- E3 ubiquitin-protein ligase RNF130
- UniProt
- Q8VEM1
- Pockets
- 4 · best druggability 0.40
Structure
1 distinct chain · 39% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | E3 ubiquitin-protein ligase RNF130 | protein | 419 | 39% helix, 17% strand | Q8VEM1 |
Pockets
4 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 113 | 0.40 | 0.76 | 21 | empty |
| 2 | 93 | 0.38 | 0.76 | 14 | empty |
| 3 | 115 | 0.34 | 0.72 | 19 | empty |
| 4 | 53 | 0.27 | 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 Q8VEM1
- Elsewhere: UniProt Q8VEM1 · AlphaFold DB Q8VEM1
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