Research workbench
AlphaFold monomer V2.0 prediction for actin-histidine N-methyltransferase (Q5ZML9)
Analyse AlphaFold monomer V2.0 prediction for actin-histidine N-methyltransferase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q5ZML9
- Type
- protein
- Length
- 593 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xd10960F956646DE8b64d3598984c91C2d5Af3D7b
- Molecule
- Actin-histidine N-methyltransferase
- UniProt
- Q5ZML9
- Pockets
- 7 · best druggability 0.80
Structure
1 distinct chain · 46% helix, 10% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Actin-histidine N-methyltransferase | protein | 593 | 46% helix, 10% strand | Q5ZML9 |
Pockets
7 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1161 | 0.80 | 0.81 | 106 | empty |
| 2 | 188 | 0.49 | 0.76 | 24 | empty |
| 3 | 64 | 0.44 | 0.83 | 19 | empty |
| 4 | 120 | 0.44 | 0.77 | 15 | empty |
| 5 | 92 | 0.39 | 0.77 | 18 | 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 Q5ZML9
- Elsewhere: UniProt Q5ZML9 · AlphaFold DB Q5ZML9
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