Research workbench
AlphaFold monomer V2.0 prediction for shikimate dehydrogenase (NADP(+)) (A5I4X1)
Analyse AlphaFold monomer V2.0 prediction for shikimate dehydrogenase (NADP(+)) (A5I4X1) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- A5I4X1
- Type
- protein
- Length
- 258 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xCF9F00f1Afe6fF25D997501B56BB9EF23263a32C
- Molecule
- Shikimate dehydrogenase (NADP(+))
- UniProt
- A5I4X1
- Pockets
- 2 · best druggability 0.70
Structure
1 distinct chain · 33% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Shikimate dehydrogenase (NADP(+)) | protein | 258 | 33% helix, 23% strand | A5I4X1 |
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 | 510 | 0.70 | 0.80 | 43 | empty |
| 2 | 66 | 0.32 | 0.76 | 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 A5I4X1
- Elsewhere: UniProt A5I4X1 · AlphaFold DB A5I4X1
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