Research workbench
AlphaFold monomer V2.0 prediction for NADPH dehydrogenase (B7ITF9)
Analyse AlphaFold monomer V2.0 prediction for NADPH dehydrogenase (B7ITF9) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- B7ITF9
- Type
- protein
- Length
- 345 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xE2e7aE2D5d6d88622B66a6Ed3Db927F2F71b3d50
- Molecule
- NADPH dehydrogenase
- UniProt
- B7ITF9
- Pockets
- 2 · best druggability 0.53
Structure
1 distinct chain · 37% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | NADPH dehydrogenase | protein | 345 | 37% helix, 16% strand | B7ITF9 |
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 | 240 | 0.53 | 0.76 | 33 | empty |
| 2 | 53 | 0.31 | 0.77 | 14 | 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 B7ITF9
- Elsewhere: UniProt B7ITF9 · AlphaFold DB B7ITF9
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