Research workbench
AlphaFold monomer V2.0 prediction for ketol-acid reductoisomerase (NADP(+)) (A4VPI6)
Analyse AlphaFold monomer V2.0 prediction for ketol-acid reductoisomerase (NADP(+))… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- A4VPI6
- Type
- protein
- Length
- 338 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x7E98f6A02556dc8C8E41BFbaE3d5CEB7162e02a2
- Molecule
- Ketol-acid reductoisomerase (NADP(+))
- UniProt
- A4VPI6
- Pockets
- 4 · best druggability 0.59
Structure
1 distinct chain · 60% helix, 12% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Ketol-acid reductoisomerase (NADP(+)) | protein | 338 | 60% helix, 12% strand | A4VPI6 |
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 396 | 0.59 | 0.75 | 42 | empty |
| 2 | 282 | 0.50 | 0.73 | 27 | empty |
| 3 | 111 | 0.36 | 0.73 | 13 | empty |
| 4 | 57 | 0.25 | 0.72 | 13 | 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 A4VPI6
- Elsewhere: UniProt A4VPI6 · AlphaFold DB A4VPI6
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