Research workbench
AlphaFold monomer V2.0 prediction for E3 ubiquitin-protein ligase RNF169 (Q8NCN4)
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
- Q8NCN4
- Type
- protein
- Length
- 708 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x79a905d858Ce72991FD6E7a9C6498620f42E146D
- Molecule
- E3 ubiquitin-protein ligase RNF169
- UniProt
- Q8NCN4
- Pockets
- 3 · best druggability 0.51
Structure
1 distinct chain · 20% helix, 1% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | E3 ubiquitin-protein ligase RNF169 | protein | 708 | 20% helix, 1% strand | Q8NCN4 |
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 191 | 0.51 | 0.77 | 27 | empty |
| 2 | 94 | 0.35 | 0.74 | 16 | empty |
| 3 | 80 | 0.30 | 0.73 | 21 | empty |
Modifications
Observed in the structure: 1 disulfide (disulfide).
Compared structures
- 5VEY · Solution NMR structure of histone H2A-H2B mono-ubiquitylated at H2A LYS15 in complex with… · an experimental structure of the same protein · chain A against C, TM-score 0.06
- 5VEY · Solution NMR structure of histone H2A-H2B mono-ubiquitylated at H2A Lys15 in complex with… · an experimental structure of the same protein · chain A against C, TM-score 0.06
- 5GG4 · Crystal structure of USP7 with RNF169 peptide · an experimental structure of the same protein · chain A against H, TM-score 0.02
- 5GG4 · Crystal structure of USP7 with RNF169 peptide · an experimental structure of the same protein · chain A against H, TM-score 0.02
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 Q8NCN4
- Elsewhere: UniProt Q8NCN4 · AlphaFold DB Q8NCN4
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