Research workbench
AlphaFold monomer V2.0 prediction for NAD(P)H-quinone oxidoreductase subunit 5, chloroplastic (A1XG02)
Analyse AlphaFold monomer V2.0 prediction for NAD(P)H-quinone oxidoreductase subunit 5… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- A1XG02
- Type
- protein
- Length
- 740 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x738c1929c69B751bD0Be0B962D9bac20B631aAc6
- Molecule
- NAD(P)H-quinone oxidoreductase subunit 5, chloroplastic
- UniProt
- A1XG02
- Pockets
- 6 · best druggability 0.76
Structure
1 distinct chain · 70% helix, 3% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | NAD(P)H-quinone oxidoreductase subunit 5, chloroplastic | protein | 740 | 70% helix, 3% strand | A1XG02 |
Pockets
6 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 752 | 0.76 | 0.80 | 74 | empty |
| 2 | 1041 | 0.74 | 0.77 | 64 | empty |
| 3 | 269 | 0.57 | 0.77 | 37 | empty |
| 4 | 113 | 0.46 | 0.78 | 18 | empty |
| 5 | 157 | 0.44 | 0.75 | 22 | 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 A1XG02
- Elsewhere: UniProt A1XG02 · AlphaFold DB A1XG02
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