Research workbench
AlphaFold monomer V2.0 prediction for hyaluronidase (A3QVN6)
Analyse AlphaFold monomer V2.0 prediction for hyaluronidase (A3QVN6) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- A3QVN6
- Type
- protein
- Length
- 449 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x5c4adF1416281C09AE8eE1cbb80fF7e44cE86F97
- Molecule
- Hyaluronidase
- UniProt
- A3QVN6
- Pockets
- 3 · best druggability 0.52
Structure
1 distinct chain · 44% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Hyaluronidase | protein | 449 | 44% helix, 16% strand | A3QVN6 |
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 | 241 | 0.52 | 0.75 | 32 | empty |
| 2 | 129 | 0.43 | 0.76 | 18 | empty |
| 3 | 113 | 0.39 | 0.75 | 18 | 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 A3QVN6
- Elsewhere: UniProt A3QVN6 · AlphaFold DB A3QVN6
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