Research workbench
AlphaFold monomer V2.0 prediction for E3 ubiquitin-protein ligase RNF169 (E7FAP1)
Analyse AlphaFold monomer V2.0 prediction for E3 ubiquitin-protein ligase RNF169… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- E7FAP1
- Type
- protein
- Length
- 630 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xb4D2d9c96b0D792d0b77e7147D724cc1F801ae58
- Molecule
- E3 ubiquitin-protein ligase RNF169
- UniProt
- E7FAP1
- Pockets
- 2 · best druggability 0.37
Structure
1 distinct chain · 24% helix, 2% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | E3 ubiquitin-protein ligase RNF169 | protein | 630 | 24% helix, 2% strand | E7FAP1 |
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 | 100 | 0.37 | 0.75 | 17 | empty |
| 2 | 72 | 0.29 | 0.73 | 14 | 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 E7FAP1
- Elsewhere: UniProt E7FAP1 · AlphaFold DB E7FAP1
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