Research workbench
AlphaFold monomer V2.0 prediction for 1-deoxy-D-xylulose 5-phosphate reductoisomerase (A7FFH3)
Analyse AlphaFold monomer V2.0 prediction for 1-deoxy-D-xylulose 5-phosphate… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- A7FFH3
- Type
- protein
- Length
- 398 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x1ED4a68B4011314730adE976b56Ad4cA21b54dcD
- Molecule
- 1-deoxy-D-xylulose 5-phosphate reductoisomerase
- UniProt
- A7FFH3
- Pockets
- 3 · best druggability 0.73
Structure
1 distinct chain · 52% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | 1-deoxy-D-xylulose 5-phosphate reductoisomerase | protein | 398 | 52% helix, 15% strand | A7FFH3 |
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 | 391 | 0.73 | 0.84 | 65 | empty |
| 2 | 53 | 0.28 | 0.75 | 15 | empty |
| 3 | 50 | 0.27 | 0.75 | 17 | 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 A7FFH3
- Elsewhere: UniProt A7FFH3 · AlphaFold DB A7FFH3
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