Research workbench
AlphaFold monomer V2.0 prediction for ring finger protein 39 (Q9H2S5)
Analyse AlphaFold monomer V2.0 prediction for ring finger protein 39 (Q9H2S5) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q9H2S5
- Type
- protein
- Length
- 420 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x5c4adF1416281C09AE8eE1cbb80fF7e44cE86F97
- Molecule
- Ring finger protein 39
- UniProt
- Q9H2S5
- Pockets
- 5 · best druggability 0.73
Structure
1 distinct chain · 18% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Ring finger protein 39 | protein | 420 | 18% helix, 20% strand | Q9H2S5 |
Pockets
5 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 555 | 0.73 | 0.81 | 62 | empty |
| 2 | 309 | 0.73 | 0.85 | 34 | empty |
| 3 | 734 | 0.69 | 0.76 | 67 | empty |
| 4 | 114 | 0.41 | 0.76 | 22 | empty |
| 5 | 66 | 0.40 | 0.80 | 13 | 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 Q9H2S5
- Elsewhere: UniProt Q9H2S5 · AlphaFold DB Q9H2S5
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