Research workbench
AlphaFold monomer V2.0 prediction for nucleotide-binding protein SPYM51325 (A2RFM4)
Analyse AlphaFold monomer V2.0 prediction for nucleotide-binding protein SPYM51325… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- A2RFM4
- Type
- protein
- Length
- 296 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x8E72F2119bF02e08301950023b4779D3C5F1Eaaa
- Molecule
- Nucleotide-binding protein SPYM51325
- UniProt
- A2RFM4
- Pockets
- 3 · best druggability 0.54
Structure
1 distinct chain · 44% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Nucleotide-binding protein SPYM51325 | protein | 296 | 44% helix, 21% strand | A2RFM4 |
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 226 | 0.54 | 0.77 | 36 | empty |
| 2 | 80 | 0.48 | 0.83 | 19 | empty |
| 3 | 133 | 0.43 | 0.76 | 19 | 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 A2RFM4
- Elsewhere: UniProt A2RFM4 · AlphaFold DB A2RFM4
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.