Research workbench
AlphaFold monomer V2.0 prediction for RAS association domain- containing protein 1 (Q99MK9)
Analyse AlphaFold monomer V2.0 prediction for RAS association domain- containing… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q99MK9
- Type
- protein
- Length
- 340 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xf87a97E0A4bB354D834857B14296240B167cbe70
- Molecule
- RAS association domain-containing protein 1
- UniProt
- Q99MK9
- Pockets
- 6 · best druggability 0.56
Structure
1 distinct chain · 26% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | RAS association domain-containing protein 1 | protein | 340 | 26% helix, 19% strand | Q99MK9 |
Pockets
6 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 173 | 0.56 | 0.81 | 26 | empty |
| 2 | 241 | 0.56 | 0.78 | 32 | empty |
| 3 | 136 | 0.39 | 0.73 | 20 | empty |
| 4 | 65 | 0.30 | 0.74 | 9 | empty |
| 5 | 51 | 0.28 | 0.75 | 14 | 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 Q99MK9
- Elsewhere: UniProt Q99MK9 · AlphaFold DB Q99MK9
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