Research workbench
AlphaFold monomer V2.0 prediction for histidine ammonia-lyase (P0DB75)
Analyse AlphaFold monomer V2.0 prediction for histidine ammonia-lyase (P0DB75) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P0DB75
- Type
- protein
- Length
- 513 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xDabAa5473122e244d48C228e8a60D59dA35E5D2D
- Molecule
- Histidine ammonia-lyase
- UniProt
- P0DB75
- Pockets
- 3 · best druggability 0.50
Structure
1 distinct chain · 59% helix, 8% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Histidine ammonia-lyase | protein | 513 | 59% helix, 8% strand | P0DB75 |
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 | 168 | 0.50 | 0.77 | 21 | empty |
| 2 | 155 | 0.49 | 0.78 | 34 | empty |
| 3 | 57 | 0.36 | 0.79 | 15 | 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 P0DB75
- Elsewhere: UniProt P0DB75 · AlphaFold DB P0DB75
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