Research workbench
AlphaFold monomer V2.0 prediction for S-ADENOSYLMETHIONINE:TRNA ribosyltransferase-isomerase (B1HVA2)
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
- B1HVA2
- Type
- protein
- Length
- 346 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xa178cE677748B9f80A2a9921a7edc5C39EDB037A
- Molecule
- S-ADENOSYLMETHIONINE:TRNA ribosyltransferase-isomerase
- UniProt
- B1HVA2
- Pockets
- 3 · best druggability 0.76
Structure
1 distinct chain · 30% helix, 29% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | S-ADENOSYLMETHIONINE:TRNA ribosyltransferase-isomerase | protein | 346 | 30% helix, 29% strand | B1HVA2 |
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 | 314 | 0.76 | 0.88 | 48 | empty |
| 2 | 153 | 0.54 | 0.80 | 30 | empty |
| 3 | 151 | 0.46 | 0.76 | 24 | 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 B1HVA2
- Elsewhere: UniProt B1HVA2 · AlphaFold DB B1HVA2
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