Research workbench
AlphaFold monomer V2.0 prediction for actin-histidine N-methyltransferase (Q9W3U1)
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
- Q9W3U1
- Type
- protein
- Length
- 537 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x460E4e7A7290a39D7Ba2ae71B7B7CEa0ecE29BeC
- Molecule
- Actin-histidine N-methyltransferase
- UniProt
- Q9W3U1
- Pockets
- 6 · best druggability 0.76
Structure
1 distinct chain · 49% helix, 13% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Actin-histidine N-methyltransferase | protein | 537 | 49% helix, 13% strand | Q9W3U1 |
Pockets
6 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 874 | 0.76 | 0.79 | 101 | empty |
| 2 | 258 | 0.52 | 0.75 | 34 | empty |
| 3 | 50 | 0.47 | 0.86 | 16 | empty |
| 4 | 77 | 0.33 | 0.75 | 16 | empty |
| 5 | 61 | 0.30 | 0.75 | 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 Q9W3U1
- Elsewhere: UniProt Q9W3U1 · AlphaFold DB Q9W3U1
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