Research workbench
AlphaFold monomer V2.0 prediction for S-adenosylmethionine decarboxylase proenzyme (B0TI92)
Analyse AlphaFold monomer V2.0 prediction for S-adenosylmethionine decarboxylase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- B0TI92
- Type
- protein
- Length
- 290 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xdF2b063d4B94F3f46D117B1af99A846bD4a59284
- Molecule
- S-adenosylmethionine decarboxylase proenzyme
- UniProt
- B0TI92
- Pockets
- 3 · best druggability 0.44
Structure
1 distinct chain · 29% helix, 31% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | S-adenosylmethionine decarboxylase proenzyme | protein | 290 | 29% helix, 31% strand | B0TI92 |
Pockets
3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 98 | 0.44 | 0.79 | 20 | empty |
| 2 | 115 | 0.40 | 0.75 | 21 | empty |
| 3 | 51 | 0.27 | 0.74 | 12 | 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 B0TI92
- Elsewhere: UniProt B0TI92 · AlphaFold DB B0TI92
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