Research workbench
AlphaFold monomer V2.0 prediction for ring finger protein B (Q7M3S9)
Analyse AlphaFold monomer V2.0 prediction for ring finger protein B (Q7M3S9) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q7M3S9
- Type
- protein
- Length
- 943 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xd91633319BDB0a92cbC4f08DeA734Bf74C030064
- Molecule
- Ring finger protein B
- UniProt
- Q7M3S9
- Pockets
- 7 · best druggability 0.76
Structure
1 distinct chain · 29% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Ring finger protein B | protein | 943 | 29% helix, 21% strand | Q7M3S9 |
Pockets
7 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 836 | 0.76 | 0.79 | 95 | empty |
| 2 | 219 | 0.59 | 0.80 | 22 | empty |
| 3 | 359 | 0.59 | 0.76 | 37 | empty |
| 4 | 110 | 0.51 | 0.81 | 22 | empty |
| 5 | 114 | 0.36 | 0.74 | 15 | empty |
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 Q7M3S9
- Elsewhere: UniProt Q7M3S9 · AlphaFold DB Q7M3S9
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