Research workbench
AlphaFold monomer V2.0 prediction for histidine ammonia-lyase (A8HA91)
Analyse AlphaFold monomer V2.0 prediction for histidine ammonia-lyase (A8HA91) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- A8HA91
- Type
- protein
- Length
- 510 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x36171628fBe26981485F3F0fdC3eeCbF3a5Ce7b9
- Molecule
- Histidine ammonia-lyase
- UniProt
- A8HA91
- Pockets
- 3 · best druggability 0.48
Structure
1 distinct chain · 59% helix, 7% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Histidine ammonia-lyase | protein | 510 | 59% helix, 7% strand | A8HA91 |
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 | 126 | 0.48 | 0.79 | 23 | empty |
| 2 | 117 | 0.41 | 0.76 | 23 | empty |
| 3 | 59 | 0.28 | 0.74 | 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 A8HA91
- Elsewhere: UniProt A8HA91 · AlphaFold DB A8HA91
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