Research workbench
AlphaFold monomer V2.0 prediction for bifunctional NAD(P)H-hydrate repair enzyme nnr (O29407)
Analyse AlphaFold monomer V2.0 prediction for bifunctional NAD(P)H-hydrate repair… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- O29407
- Type
- protein
- Length
- 464 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xbDA05C32aD6eE153C8C5A78dfa48d7Ba25694fea
- Molecule
- Bifunctional NAD(P)H-hydrate repair enzyme nnr
- UniProt
- O29407
- Pockets
- 3 · best druggability 0.66
Structure
1 distinct chain · 43% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Bifunctional NAD(P)H-hydrate repair enzyme nnr | protein | 464 | 43% helix, 17% strand | O29407 |
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 | 251 | 0.66 | 0.83 | 30 | empty |
| 2 | 92 | 0.47 | 0.81 | 18 | empty |
| 3 | 182 | 0.46 | 0.75 | 36 | 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 O29407
- Elsewhere: UniProt O29407 · AlphaFold DB O29407
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