Research workbench
AlphaFold monomer V2.0 prediction for S-adenosylmethionine decarboxylase proenzyme (B2V2S2)
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
- B2V2S2
- Type
- protein
- Length
- 272 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x1ED4a68B4011314730adE976b56Ad4cA21b54dcD
- Molecule
- S-adenosylmethionine decarboxylase proenzyme
- UniProt
- B2V2S2
- Pockets
- 3 · best druggability 0.42
Structure
1 distinct chain · 32% helix, 31% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | S-adenosylmethionine decarboxylase proenzyme | protein | 272 | 32% helix, 31% strand | B2V2S2 |
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 | 135 | 0.42 | 0.75 | 24 | empty |
| 2 | 81 | 0.34 | 0.75 | 13 | empty |
| 3 | 66 | 0.30 | 0.74 | 18 | 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 B2V2S2
- Elsewhere: UniProt B2V2S2 · AlphaFold DB B2V2S2
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