Research workbench
AlphaFold monomer V2.0 prediction for oxygen-insensitive NAD(P)H nitroreductase (P15888)
Analyse AlphaFold monomer V2.0 prediction for oxygen-insensitive NAD(P)H nitroreductase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P15888
- Type
- protein
- Length
- 217 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x5BeA89782341f98147F2D811B063F91F0aE7D7bF
- Molecule
- Oxygen-insensitive NAD(P)H nitroreductase
- UniProt
- P15888
- Pockets
- 1 · best druggability 0.27
Structure
1 distinct chain · 54% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Oxygen-insensitive NAD(P)H nitroreductase | protein | 217 | 54% helix, 14% strand | P15888 |
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 60 | 0.27 | 0.73 | 14 | empty |
Compared structures
- 3HZN · Structure of the salmonella typhimurium nfnb dihydropteridine reductase · an experimental structure of the same protein · chain A against C, TM-score 0.99
- 3HZN · Structure of the Salmonella typhimurium nfnB dihydropteridine reductase · an experimental structure of the same protein · chain A against C, TM-score 0.99
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 P15888
- Elsewhere: UniProt P15888 · AlphaFold DB P15888
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