Research workbench
AlphaFold monomer V2.0 prediction for S-adenosylmethionine decarboxylase proenzyme (B5YZF5)
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
- B5YZF5
- Type
- protein
- Length
- 264 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x758850a3D7646b829972912E8A512268C74ceb66
- Molecule
- S-adenosylmethionine decarboxylase proenzyme
- UniProt
- B5YZF5
- Pockets
- 2 · best druggability 0.44
Structure
1 distinct chain · 30% helix, 33% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | S-adenosylmethionine decarboxylase proenzyme | protein | 264 | 30% helix, 33% strand | B5YZF5 |
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 148 | 0.44 | 0.75 | 26 | empty |
| 2 | 126 | 0.41 | 0.75 | 30 | 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 B5YZF5
- Elsewhere: UniProt B5YZF5 · AlphaFold DB B5YZF5
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