Research workbench
AlphaFold monomer V2.0 prediction for multiple RNA-binding domain- containing protein 1 (Q5BGA9)
Analyse AlphaFold monomer V2.0 prediction for multiple RNA-binding domain- containing… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q5BGA9
- Type
- protein
- Length
- 819 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x6DAA77C4263E74E745cA9c4D8E291e57e8991Cf5
- Molecule
- Multiple RNA-binding domain-containing protein 1
- UniProt
- Q5BGA9
- Pockets
- 4 · best druggability 0.64
Structure
1 distinct chain · 29% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Multiple RNA-binding domain-containing protein 1 | protein | 819 | 29% helix, 18% strand | Q5BGA9 |
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 581 | 0.64 | 0.75 | 78 | empty |
| 2 | 115 | 0.42 | 0.76 | 16 | empty |
| 3 | 97 | 0.36 | 0.75 | 28 | empty |
| 4 | 64 | 0.32 | 0.75 | 16 | 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 Q5BGA9
- Elsewhere: UniProt Q5BGA9 · AlphaFold DB Q5BGA9
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