MolNFT v1 · #536439 · protein
AlphaFold monomer V2.0 prediction for sporulation protein ypeb (P59106)
P59106: “AlphaFold monomer V2.0 prediction for sporulation protein ypeb (P59106)”. 5 pockets (best druggability 0.42). MolNFT v1 #536439 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- Accession
- P59106
- Type
- protein
- Length
- 447 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x4b55D2279Ab6D7ad49C3d2b3D16574252E13E63D
- Molecule
- Sporulation protein ypeb
- UniProt
- P59106
- Pockets
- 5 · best druggability 0.42
Structure
1 distinct chain · 44% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Sporulation protein ypeb | protein | 447 | 44% helix, 23% strand | P59106 |
Pockets
5 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 99 | 0.42 | 0.78 | 22 | empty |
| 2 | 128 | 0.41 | 0.75 | 17 | empty |
| 3 | 74 | 0.35 | 0.76 | 14 | empty |
| 4 | 57 | 0.33 | 0.77 | 12 | empty |
| 5 | 51 | 0.28 | 0.74 | 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 P59106
- Elsewhere: UniProt P59106 · AlphaFold DB P59106
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