Research workbench
AlphaFold monomer V2.0 prediction for protein arginine N-methyltransferase 2 (Q4X1R1)
Analyse AlphaFold monomer V2.0 prediction for protein arginine N-methyltransferase 2… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q4X1R1
- Type
- protein
- Length
- 424 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x7782F4817b37743d738e9aF842bf74bd50f2015E
- Molecule
- Protein arginine N-methyltransferase 2
- UniProt
- Q4X1R1
- Pockets
- 4 · best druggability 0.78
Structure
1 distinct chain · 40% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein arginine N-methyltransferase 2 | protein | 424 | 40% helix, 14% strand | Q4X1R1 |
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 758 | 0.78 | 0.82 | 52 | empty |
| 2 | 73 | 0.70 | 0.95 | 21 | empty |
| 3 | 70 | 0.35 | 0.77 | 13 | empty |
| 4 | 63 | 0.27 | 0.73 | 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 Q4X1R1
- Elsewhere: UniProt Q4X1R1 · AlphaFold DB Q4X1R1
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