Research workbench
AlphaFold monomer V2.0 prediction for probable manganese-dependent inorganic pyrophosphatase (B1YLU2)
Analyse AlphaFold monomer V2.0 prediction for probable manganese-dependent inorganic… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- B1YLU2
- Type
- protein
- Length
- 311 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xa2a8313a9ac1C6C2Fd647eb71D26A934AC647886
- Molecule
- Probable manganese-dependent inorganic pyrophosphatase
- UniProt
- B1YLU2
- Pockets
- 4 · best druggability 0.79
Structure
1 distinct chain · 43% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Probable manganese-dependent inorganic pyrophosphatase | protein | 311 | 43% helix, 20% strand | B1YLU2 |
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 | 167 | 0.79 | 0.95 | 33 | empty |
| 2 | 144 | 0.45 | 0.77 | 26 | empty |
| 3 | 55 | 0.40 | 0.81 | 15 | empty |
| 4 | 74 | 0.40 | 0.79 | 23 | 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 B1YLU2
- Elsewhere: UniProt B1YLU2 · AlphaFold DB B1YLU2
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