Research workbench
AlphaFold monomer V2.0 prediction for ADP-dependent (S)-NAD(P)H-hydrate dehydratase (D2RXF6)
Analyse AlphaFold monomer V2.0 prediction for ADP-dependent (S)-NAD(P)H-hydrate… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- D2RXF6
- Type
- protein
- Length
- 257 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x0EA189b2343A464f560b44103f6A3396Da1dA8a9
- Molecule
- ADP-dependent (S)-NAD(P)H-hydrate dehydratase
- UniProt
- D2RXF6
- Pockets
- 2 · best druggability 0.53
Structure
1 distinct chain · 50% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | ADP-dependent (S)-NAD(P)H-hydrate dehydratase | protein | 257 | 50% helix, 17% strand | D2RXF6 |
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 | 231 | 0.53 | 0.77 | 38 | empty |
| 2 | 54 | 0.28 | 0.75 | 12 | 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 D2RXF6
- Elsewhere: UniProt D2RXF6 · AlphaFold DB D2RXF6
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