Research workbench
AlphaFold monomer V2.0 prediction for S-ADENOSYLMETHIONINE:TRNA ribosyltransferase-isomerase (A5FMM5)
Analyse AlphaFold monomer V2.0 prediction for S-ADENOSYLMETHIONINE:TRNA… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- A5FMM5
- Type
- protein
- Length
- 349 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xf87a97E0A4bB354D834857B14296240B167cbe70
- Molecule
- S-ADENOSYLMETHIONINE:TRNA ribosyltransferase-isomerase
- UniProt
- A5FMM5
- Pockets
- 2 · best druggability 0.56
Structure
1 distinct chain · 30% helix, 30% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | S-ADENOSYLMETHIONINE:TRNA ribosyltransferase-isomerase | protein | 349 | 30% helix, 30% strand | A5FMM5 |
Pockets
2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 224 | 0.56 | 0.78 | 29 | empty |
| 2 | 248 | 0.56 | 0.78 | 31 | 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 A5FMM5
- Elsewhere: UniProt A5FMM5 · AlphaFold DB A5FMM5
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