Research workbench
AlphaFold monomer V2.0 prediction for S-adenosylmethionine synthase (P93254)
Analyse AlphaFold monomer V2.0 prediction for S-adenosylmethionine synthase (P93254) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P93254
- Type
- protein
- Length
- 392 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x4450b8770f8579152a0dD84fBd7622763A5eC221
- Molecule
- S-adenosylmethionine synthase
- UniProt
- P93254
- Pockets
- 4 · best druggability 0.52
Structure
1 distinct chain · 34% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | S-adenosylmethionine synthase | protein | 392 | 34% helix, 26% strand | P93254 |
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 102 | 0.52 | 0.82 | 20 | empty |
| 2 | 65 | 0.38 | 0.79 | 12 | empty |
| 3 | 52 | 0.31 | 0.77 | 13 | empty |
| 4 | 60 | 0.28 | 0.74 | 14 | 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 P93254
- Elsewhere: UniProt P93254 · AlphaFold DB P93254
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