Research workbench
AlphaFold monomer V2.0 prediction for sporulation protein ypeb (P38490)
Analyse AlphaFold monomer V2.0 prediction for sporulation protein ypeb (P38490) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P38490
- Type
- protein
- Length
- 450 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xf87a97E0A4bB354D834857B14296240B167cbe70
- Molecule
- Sporulation protein ypeb
- UniProt
- P38490
- Pockets
- 7 · best druggability 0.76
Structure
1 distinct chain · 43% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Sporulation protein ypeb | protein | 450 | 43% helix, 22% strand | P38490 |
Pockets
7 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1053 | 0.76 | 0.78 | 102 | empty |
| 2 | 229 | 0.57 | 0.79 | 29 | empty |
| 3 | 94 | 0.50 | 0.82 | 16 | empty |
| 4 | 150 | 0.44 | 0.75 | 27 | empty |
| 5 | 62 | 0.35 | 0.77 | 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 P38490
- Elsewhere: UniProt P38490 · AlphaFold DB P38490
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