Research workbench
AlphaFold monomer V2.0 prediction for shikimate dehydrogenase (NADP(+)) (C5BF12)
Analyse AlphaFold monomer V2.0 prediction for shikimate dehydrogenase (NADP(+)) (C5BF12) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- C5BF12
- Type
- protein
- Length
- 271 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xb10B578A27bBa6Cdba3967F273CC1582b84a5908
- Molecule
- Shikimate dehydrogenase (NADP(+))
- UniProt
- C5BF12
- Pockets
- 1 · best druggability 0.68
Structure
1 distinct chain · 42% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Shikimate dehydrogenase (NADP(+)) | protein | 271 | 42% helix, 21% strand | C5BF12 |
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 494 | 0.68 | 0.79 | 50 | 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 C5BF12
- Elsewhere: UniProt C5BF12 · AlphaFold DB C5BF12
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