Research workbench
AlphaFold monomer V2.0 prediction for actin-histidine N-methyltransferase (A9X1D0)
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
- A9X1D0
- Type
- protein
- Length
- 595 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xa178cE677748B9f80A2a9921a7edc5C39EDB037A
- Molecule
- Actin-histidine N-methyltransferase
- UniProt
- A9X1D0
- Pockets
- 10 · best druggability 0.68
Structure
1 distinct chain · 45% helix, 10% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Actin-histidine N-methyltransferase | protein | 595 | 45% helix, 10% strand | A9X1D0 |
Pockets
10 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 479 | 0.68 | 0.79 | 50 | empty |
| 2 | 532 | 0.65 | 0.76 | 54 | empty |
| 3 | 112 | 0.48 | 0.80 | 17 | empty |
| 4 | 112 | 0.43 | 0.77 | 15 | empty |
| 5 | 120 | 0.42 | 0.76 | 19 | 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 A9X1D0
- Elsewhere: UniProt A9X1D0 · AlphaFold DB A9X1D0
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