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AlphaFold monomer V2.0 prediction for bifunctional NAD(P)H-hydrate repair enzyme nnr (B1L3W1)
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
- B1L3W1
- Type
- protein
- Length
- 515 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x6227512B0B04f05c48A3f9Bb2A26C737dAb650E8
- Molecule
- Bifunctional NAD(P)H-hydrate repair enzyme nnr
- UniProt
- B1L3W1
- Pockets
- 3 · best druggability 0.64
Structure
1 distinct chain · 47% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Bifunctional NAD(P)H-hydrate repair enzyme nnr | protein | 515 | 47% helix, 17% strand | B1L3W1 |
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 226 | 0.64 | 0.82 | 26 | empty |
| 2 | 271 | 0.56 | 0.77 | 45 | empty |
| 3 | 65 | 0.29 | 0.74 | 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 B1L3W1
- Elsewhere: UniProt B1L3W1 · AlphaFold DB B1L3W1
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