Research workbench
AlphaFold monomer V2.0 prediction for isopentenyl-diphosphate delta- isomerase (Q9HHE4)
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
- Q9HHE4
- Type
- protein
- Length
- 360 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x8A95d18E43Cd84939F8B498D22C930eE66984B91
- Molecule
- Isopentenyl-diphosphate delta-isomerase
- UniProt
- Q9HHE4
- Pockets
- 3 · best druggability 0.84
Structure
1 distinct chain · 50% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Isopentenyl-diphosphate delta-isomerase | protein | 360 | 50% helix, 14% strand | Q9HHE4 |
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 | 339 | 0.84 | 0.94 | 52 | empty |
| 2 | 105 | 0.36 | 0.74 | 21 | empty |
| 3 | 60 | 0.28 | 0.74 | 16 | 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 Q9HHE4
- Elsewhere: UniProt Q9HHE4 · AlphaFold DB Q9HHE4
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