Research workbench
AlphaFold monomer V2.0 prediction for isopentenyl-diphosphate delta- isomerase (C3P586)
Analyse AlphaFold monomer V2.0 prediction for isopentenyl-diphosphate delta- isomerase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- C3P586
- Type
- protein
- Length
- 349 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xA81476e932072E01982403F6C56fd30fc8575e48
- Molecule
- Isopentenyl-diphosphate delta-isomerase
- UniProt
- C3P586
- Pockets
- 3 · best druggability 0.81
Structure
1 distinct chain · 48% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Isopentenyl-diphosphate delta-isomerase | protein | 349 | 48% helix, 14% strand | C3P586 |
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 381 | 0.81 | 0.90 | 55 | empty |
| 2 | 127 | 0.41 | 0.75 | 21 | empty |
| 3 | 61 | 0.27 | 0.73 | 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 C3P586
- Elsewhere: UniProt C3P586 · AlphaFold DB C3P586
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