Research workbench
AlphaFold monomer V2.0 prediction for D-histidine 2-aminobutanoyltransferase (A0A0H3JXA8)
Analyse AlphaFold monomer V2.0 prediction for D-histidine 2-aminobutanoyltransferase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- A0A0H3JXA8
- Type
- protein
- Length
- 272 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xF8cD1d8d93E9783063700De244A6e3cf6A195579
- Molecule
- D-histidine 2-aminobutanoyltransferase
- Pockets
- 1 · best druggability 0.73
Structure
1 distinct chain · 52% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | D-histidine 2-aminobutanoyltransferase | protein | 272 | 52% helix, 14% strand | — |
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 315 | 0.73 | 0.86 | 46 | empty |
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
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