Research workbench
AlphaFold monomer V2.0 prediction for S-adenosylmethionine decarboxylase proenzyme (Q3Z5P0)
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
- Q3Z5P0
- Type
- protein
- Length
- 264 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x0D671490EE06E75975e90D7F99F73B20BE618744
- Molecule
- S-adenosylmethionine decarboxylase proenzyme
- UniProt
- Q3Z5P0
- Pockets
- 4 · best druggability 0.47
Structure
1 distinct chain · 32% helix, 33% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | S-adenosylmethionine decarboxylase proenzyme | protein | 264 | 32% helix, 33% strand | Q3Z5P0 |
Pockets
4 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 183 | 0.47 | 0.75 | 26 | empty |
| 2 | 75 | 0.36 | 0.76 | 21 | empty |
| 3 | 58 | 0.29 | 0.74 | 16 | empty |
| 4 | 55 | 0.27 | 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 Q3Z5P0
- Elsewhere: UniProt Q3Z5P0 · AlphaFold DB Q3Z5P0
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