Research workbench
AlphaFold monomer V2.0 prediction for S-adenosylmethionine decarboxylase proenzyme (Q9M4D8)
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
- Q9M4D8
- Type
- protein
- Length
- 353 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xBF0D2e107Ce1EcD2C4369B042274201DB719AaAF
- Molecule
- S-adenosylmethionine decarboxylase proenzyme
- UniProt
- Q9M4D8
- Pockets
- 2 · best druggability 0.63
Structure
1 distinct chain · 23% helix, 34% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | S-adenosylmethionine decarboxylase proenzyme | protein | 353 | 23% helix, 34% strand | Q9M4D8 |
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 | 176 | 0.63 | 0.84 | 38 | empty |
| 2 | 162 | 0.53 | 0.80 | 27 | 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 Q9M4D8
- Elsewhere: UniProt Q9M4D8 · AlphaFold DB Q9M4D8
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