Research workbench
AlphaFold monomer V2.0 prediction for E3 ubiquitin-protein ligase RNF13 (Q66HG0)
Analyse AlphaFold monomer V2.0 prediction for E3 ubiquitin-protein ligase RNF13 (Q66HG0) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q66HG0
- Type
- protein
- Length
- 380 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x53ef4eA89edf91901402D21891094e22555c6D4C
- Molecule
- E3 ubiquitin-protein ligase RNF13
- UniProt
- Q66HG0
- Pockets
- 3 · best druggability 0.39
Structure
1 distinct chain · 28% helix, 13% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | E3 ubiquitin-protein ligase RNF13 | protein | 380 | 28% helix, 13% strand | Q66HG0 |
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 | 86 | 0.39 | 0.76 | 18 | empty |
| 2 | 97 | 0.35 | 0.74 | 17 | empty |
| 3 | 74 | 0.35 | 0.77 | 18 | 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 Q66HG0
- Elsewhere: UniProt Q66HG0 · AlphaFold DB Q66HG0
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