Research workbench
AlphaFold monomer V2.0 prediction for bifunctional protein hlde (A9N5X8)
Analyse AlphaFold monomer V2.0 prediction for bifunctional protein hlde (A9N5X8) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- A9N5X8
- Type
- protein
- Length
- 477 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xf15ee9678a76Fa6d624D70b80730d9238AFAaBa2
- Molecule
- Bifunctional protein hlde
- UniProt
- A9N5X8
- Pockets
- 4 · best druggability 0.60
Structure
1 distinct chain · 38% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Bifunctional protein hlde | protein | 477 | 38% helix, 23% strand | A9N5X8 |
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 340 | 0.60 | 0.77 | 34 | empty |
| 2 | 283 | 0.57 | 0.77 | 41 | empty |
| 3 | 107 | 0.36 | 0.74 | 19 | empty |
| 4 | 93 | 0.32 | 0.72 | 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 A9N5X8
- Elsewhere: UniProt A9N5X8 · AlphaFold DB A9N5X8
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