Research workbench
AlphaFold monomer V2.0 prediction for alpha N-terminal protein methyltransferase 1 (A2XMJ1)
Analyse AlphaFold monomer V2.0 prediction for alpha N-terminal protein… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- A2XMJ1
- Type
- protein
- Length
- 307 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x4Dff1DBB225A3491870Fd31Ec92D348E5c96AE0b
- Molecule
- Alpha N-terminal protein methyltransferase 1
- UniProt
- A2XMJ1
- Pockets
- 3 · best druggability 0.78
Structure
1 distinct chain · 32% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Alpha N-terminal protein methyltransferase 1 | protein | 307 | 32% helix, 21% strand | A2XMJ1 |
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 431 | 0.78 | 0.86 | 50 | empty |
| 2 | 63 | 0.32 | 0.76 | 14 | empty |
| 3 | 60 | 0.31 | 0.76 | 16 | 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 A2XMJ1
- Elsewhere: UniProt A2XMJ1 · AlphaFold DB A2XMJ1
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