Research workbench
AlphaFold monomer V2.0 prediction for trans-3-hydroxy-L-proline dehydratase (A0NXQ9)
Analyse AlphaFold monomer V2.0 prediction for trans-3-hydroxy-L-proline dehydratase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- A0NXQ9
- Type
- protein
- Length
- 341 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x2d26a86cbE380Fd92850FC0D1EFb1fe1c7915b16
- Molecule
- Trans-3-hydroxy-L-proline dehydratase
- UniProt
- A0NXQ9
- Pockets
- 3 · best druggability 0.44
Structure
1 distinct chain · 19% helix, 44% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Trans-3-hydroxy-L-proline dehydratase | protein | 341 | 19% helix, 44% strand | A0NXQ9 |
Pockets
3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 103 | 0.44 | 0.78 | 16 | empty |
| 2 | 105 | 0.37 | 0.75 | 25 | empty |
| 3 | 82 | 0.33 | 0.74 | 20 | 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 A0NXQ9
- Elsewhere: UniProt A0NXQ9 · AlphaFold DB A0NXQ9
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.