Research workbench
AlphaFold monomer V2.0 prediction for histidine ammonia-lyase (Q1Q9E4)
Analyse AlphaFold monomer V2.0 prediction for histidine ammonia-lyase (Q1Q9E4) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q1Q9E4
- Type
- protein
- Length
- 520 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xbff27Dc0a932A6E0d9Fe883AAbD1BF27bB95A69F
- Molecule
- Histidine ammonia-lyase
- UniProt
- Q1Q9E4
- Pockets
- 4 · best druggability 0.45
Structure
1 distinct chain · 58% helix, 8% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Histidine ammonia-lyase | protein | 520 | 58% helix, 8% strand | Q1Q9E4 |
Pockets
4 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 130 | 0.45 | 0.77 | 23 | empty |
| 2 | 105 | 0.40 | 0.76 | 20 | empty |
| 3 | 55 | 0.30 | 0.75 | 14 | empty |
| 4 | 56 | 0.28 | 0.75 | 16 | 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 Q1Q9E4
- Elsewhere: UniProt Q1Q9E4 · AlphaFold DB Q1Q9E4
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