Research workbench
AlphaFold monomer V2.0 prediction for UPF0210 protein LLMG_1581 (A2RLI8)
Analyse AlphaFold monomer V2.0 prediction for UPF0210 protein LLMG_1581 (A2RLI8) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- A2RLI8
- Type
- protein
- Length
- 445 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x025f3b1a898b05AD2731bE6Ab72687b5920c4A3F
- Molecule
- UPF0210 protein LLMG_1581
- UniProt
- A2RLI8
- Pockets
- 4 · best druggability 0.53
Structure
1 distinct chain · 45% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | UPF0210 protein LLMG_1581 | protein | 445 | 45% helix, 19% strand | A2RLI8 |
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 | 67 | 0.53 | 0.86 | 27 | empty |
| 2 | 66 | 0.34 | 0.77 | 14 | empty |
| 3 | 51 | 0.34 | 0.78 | 10 | empty |
| 4 | 63 | 0.34 | 0.76 | 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 A2RLI8
- Elsewhere: UniProt A2RLI8 · AlphaFold DB A2RLI8
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