Research workbench
AlphaFold monomer V2.0 prediction for phospholipase A2 heteromtoxin (P0DMI6)
Analyse AlphaFold monomer V2.0 prediction for phospholipase A2 heteromtoxin (P0DMI6) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P0DMI6
- Type
- protein
- Length
- 167 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x6F9f9CD1Df14e89bB8FDF55C2ABa04A409c977B4
- Molecule
- Phospholipase A2 heteromtoxin
- UniProt
- P0DMI6
- Pockets
- 2 · best druggability 0.62
Structure
1 distinct chain · 37% helix, 12% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Phospholipase A2 heteromtoxin | protein | 167 | 37% helix, 12% strand | P0DMI6 |
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 297 | 0.62 | 0.80 | 38 | empty |
| 2 | 59 | 0.33 | 0.77 | 12 | empty |
Modifications
Observed in the structure: 5 disulfide (disulfide).
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 P0DMI6
- Elsewhere: UniProt P0DMI6 · AlphaFold DB P0DMI6
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