Research workbench
AlphaFold monomer V2.0 prediction for radical S-adenosyl methionine domain-containing protein 1, mitochondrial (A4IGH2)
Analyse AlphaFold monomer V2.0 prediction for radical S-adenosyl methionine… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- A4IGH2
- Type
- protein
- Length
- 444 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x5881B09f2D8e743400698633641fc1cD2Ed2BE6F
- Molecule
- Radical S-adenosyl methionine domain-containing protein 1, mitochondrial
- UniProt
- A4IGH2
- Pockets
- 3 · best druggability 0.75
Structure
1 distinct chain · 41% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Radical S-adenosyl methionine domain-containing protein 1, mitochondrial | protein | 444 | 41% helix, 20% strand | A4IGH2 |
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 | 822 | 0.75 | 0.79 | 81 | empty |
| 2 | 121 | 0.43 | 0.76 | 16 | empty |
| 3 | 99 | 0.41 | 0.77 | 28 | 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 A4IGH2
- Elsewhere: UniProt A4IGH2 · AlphaFold DB A4IGH2
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