Research workbench
AlphaFold monomer V2.0 prediction for E3 ubiquitin-protein ligase RNF43 (Q5NCP0)
Analyse AlphaFold monomer V2.0 prediction for E3 ubiquitin-protein ligase RNF43 (Q5NCP0) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q5NCP0
- Type
- protein
- Length
- 784 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x97EfFf2d74994e28D3b69b1503Bd9c292B2Df480
- Molecule
- E3 ubiquitin-protein ligase RNF43
- UniProt
- Q5NCP0
- Pockets
- 3 · best druggability 0.58
Structure
1 distinct chain · 17% helix, 8% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | E3 ubiquitin-protein ligase RNF43 | protein | 784 | 17% helix, 8% strand | Q5NCP0 |
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 369 | 0.58 | 0.75 | 35 | empty |
| 2 | 99 | 0.51 | 0.82 | 19 | empty |
| 3 | 93 | 0.35 | 0.74 | 12 | 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 Q5NCP0
- Elsewhere: UniProt Q5NCP0 · AlphaFold DB Q5NCP0
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