Research workbench
AlphaFold monomer V2.0 prediction for S-adenosyl-L-methionine- dependent diels-alderase ilid (P0DO33)
Analyse AlphaFold monomer V2.0 prediction for S-adenosyl-L-methionine- dependent… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P0DO33
- Type
- protein
- Length
- 244 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xa73BAb1DabE4333A884D03393eAa10c3B4215494
- Molecule
- S-adenosyl-L-methionine-dependent diels-alderase ilid
- UniProt
- P0DO33
- Pockets
- 2 · best druggability 0.82
Structure
1 distinct chain · 40% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | S-adenosyl-L-methionine-dependent diels-alderase ilid | protein | 244 | 40% helix, 14% strand | P0DO33 |
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1011 | 0.82 | 0.83 | 86 | empty |
| 2 | 93 | 0.34 | 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 P0DO33
- Elsewhere: UniProt P0DO33 · AlphaFold DB P0DO33
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