Research workbench
AlphaFold monomer V2.0 prediction for ADP-dependent (S)-NAD(P)H-hydrate dehydratase (P96051)
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
- P96051
- Type
- protein
- Length
- 278 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x4191C26e46CD82B225Fe6ff6B36C2C4F7128Af41
- Molecule
- ADP-dependent (S)-NAD(P)H-hydrate dehydratase
- UniProt
- P96051
- Pockets
- 3 · best druggability 0.46
Structure
1 distinct chain · 49% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | ADP-dependent (S)-NAD(P)H-hydrate dehydratase | protein | 278 | 49% helix, 15% strand | P96051 |
Pockets
3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 174 | 0.46 | 0.76 | 36 | empty |
| 2 | 70 | 0.40 | 0.80 | 16 | empty |
| 3 | 88 | 0.36 | 0.75 | 20 | 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 P96051
- Elsewhere: UniProt P96051 · AlphaFold DB P96051
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