Research workbench
AlphaFold monomer V2.0 prediction for trans-O- hydroxybenzylidenepyruvate hydratase-aldolase (P0A142)
Analyse AlphaFold monomer V2.0 prediction for trans-O- hydroxybenzylidenepyruvate… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P0A142
- Type
- protein
- Length
- 334 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x5BeA89782341f98147F2D811B063F91F0aE7D7bF
- Molecule
- Trans-O-hydroxybenzylidenepyruvate hydratase-aldolase
- UniProt
- P0A142
- Pockets
- 3 · best druggability 0.61
Structure
1 distinct chain · 51% helix, 10% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Trans-O-hydroxybenzylidenepyruvate hydratase-aldolase | protein | 334 | 51% helix, 10% strand | P0A142 |
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 | 129 | 0.61 | 0.85 | 25 | empty |
| 2 | 160 | 0.53 | 0.79 | 27 | empty |
| 3 | 117 | 0.42 | 0.76 | 26 | 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 P0A142
- Elsewhere: UniProt P0A142 · AlphaFold DB P0A142
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