Research workbench
AlphaFold monomer V2.0 prediction for protein arginine methyltransferase NDUFAF7, mitochondrial (Q7L592)
Analyse AlphaFold monomer V2.0 prediction for protein arginine methyltransferase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q7L592
- Type
- protein
- Length
- 441 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x0eE054AC843F2F5F024A81f2c7026947A09008Ac
- Molecule
- Protein arginine methyltransferase NDUFAF7, mitochondrial
- UniProt
- Q7L592
- Pockets
- 3 · best druggability 0.75
Structure
1 distinct chain · 34% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein arginine methyltransferase NDUFAF7, mitochondrial | protein | 441 | 34% helix, 22% strand | Q7L592 |
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 570 | 0.75 | 0.82 | 60 | empty |
| 2 | 318 | 0.53 | 0.74 | 36 | empty |
| 3 | 59 | 0.30 | 0.75 | 11 | 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 Q7L592
- Elsewhere: UniProt Q7L592 · AlphaFold DB Q7L592
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