Research workbench
AlphaFold monomer V2.0 prediction for probable manganese-dependent inorganic pyrophosphatase (C4L0S9)
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
- C4L0S9
- Type
- protein
- Length
- 309 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x6308DDF1510b8a81bb24FEB0c698521800724898
- Molecule
- Probable manganese-dependent inorganic pyrophosphatase
- UniProt
- C4L0S9
- Pockets
- 3 · best druggability 0.76
Structure
1 distinct chain · 42% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Probable manganese-dependent inorganic pyrophosphatase | protein | 309 | 42% helix, 20% strand | C4L0S9 |
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 | 205 | 0.76 | 0.91 | 33 | empty |
| 2 | 89 | 0.48 | 0.82 | 23 | empty |
| 3 | 55 | 0.31 | 0.76 | 15 | 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 C4L0S9
- Elsewhere: UniProt C4L0S9 · AlphaFold DB C4L0S9
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