Research workbench
AlphaFold monomer V2.0 prediction for endospore coat-associated protein yhed (O07545)
Analyse AlphaFold monomer V2.0 prediction for endospore coat-associated protein yhed… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- O07545
- Type
- protein
- Length
- 453 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xB2De55958Eb8f6D034F34AcD450a665515111eE9
- Molecule
- Endospore coat-associated protein yhed
- UniProt
- O07545
- Pockets
- 3 · best druggability 0.76
Structure
1 distinct chain · 32% helix, 34% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Endospore coat-associated protein yhed | protein | 453 | 32% helix, 34% strand | O07545 |
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 586 | 0.76 | 0.82 | 71 | empty |
| 2 | 71 | 0.50 | 0.85 | 17 | empty |
| 3 | 101 | 0.38 | 0.75 | 18 | 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 O07545
- Elsewhere: UniProt O07545 · AlphaFold DB O07545
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