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AlphaFold monomer V2.0 prediction for ATP-dependent (S)-NAD(P)H-hydrate dehydratase 2 (E3L9T1)
Analyse AlphaFold monomer V2.0 prediction for ATP-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
- E3L9T1
- Type
- protein
- Length
- 346 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x76Eb9c945D94E1C3742218E975e22f8713c0432f
- Molecule
- ATP-dependent (S)-NAD(P)H-hydrate dehydratase 2
- UniProt
- E3L9T1
- Pockets
- 3 · best druggability 0.56
Structure
1 distinct chain · 49% helix, 11% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | ATP-dependent (S)-NAD(P)H-hydrate dehydratase 2 | protein | 346 | 49% helix, 11% strand | E3L9T1 |
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 292 | 0.56 | 0.77 | 37 | empty |
| 2 | 166 | 0.48 | 0.77 | 14 | empty |
| 3 | 91 | 0.39 | 0.77 | 15 | 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 E3L9T1
- Elsewhere: UniProt E3L9T1 · AlphaFold DB E3L9T1
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