Research workbench
AlphaFold monomer V2.0 prediction for actin-histidine N-methyltransferase (Q91WC0)
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
- Q91WC0
- Type
- protein
- Length
- 594 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xF8cD1d8d93E9783063700De244A6e3cf6A195579
- Molecule
- Actin-histidine N-methyltransferase
- UniProt
- Q91WC0
- Pockets
- 8 · best druggability 0.80
Structure
1 distinct chain · 45% helix, 10% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Actin-histidine N-methyltransferase | protein | 594 | 45% helix, 10% strand | Q91WC0 |
Pockets
8 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 911 | 0.80 | 0.82 | 92 | empty |
| 2 | 195 | 0.54 | 0.79 | 35 | empty |
| 3 | 188 | 0.47 | 0.75 | 30 | empty |
| 4 | 109 | 0.41 | 0.76 | 15 | empty |
| 5 | 84 | 0.38 | 0.77 | 15 | 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 Q91WC0
- Elsewhere: UniProt Q91WC0 · AlphaFold DB Q91WC0
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