MolNFT v1 · #329752 · protein
AlphaFold monomer V2.0 prediction for S-ADENOSYLMETHIONINE:TRNA ribosyltransferase-isomerase (A5N205)
A5N205: “AlphaFold monomer V2.0 prediction for S-ADENOSYLMETHIONINE:TRNA ribosyltransferase-isomerase (A5N205)”. 2 pockets (best druggability 0.73). MolNFT v1 #329752 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- Accession
- A5N205
- Type
- protein
- Length
- 341 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xdF2b063d4B94F3f46D117B1af99A846bD4a59284
- Molecule
- S-ADENOSYLMETHIONINE:TRNA ribosyltransferase-isomerase
- UniProt
- A5N205
- Pockets
- 2 · best druggability 0.73
Structure
1 distinct chain · 30% helix, 29% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | S-ADENOSYLMETHIONINE:TRNA ribosyltransferase-isomerase | protein | 341 | 30% helix, 29% strand | A5N205 |
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 | 274 | 0.73 | 0.87 | 45 | empty |
| 2 | 397 | 0.59 | 0.76 | 49 | 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 A5N205
- Elsewhere: UniProt A5N205 · AlphaFold DB A5N205
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