Research workbench
AlphaFold monomer V2.0 prediction for NAD(P)H-quinone oxidoreductase subunit 2 a, chloroplastic (P0CD12)
Analyse AlphaFold monomer V2.0 prediction for NAD(P)H-quinone oxidoreductase subunit 2… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P0CD12
- Type
- protein
- Length
- 510 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x7C5991B66CA84425AC947F3bE4428892A9f521dc
- Molecule
- NAD(P)H-quinone oxidoreductase subunit 2 a, chloroplastic
- UniProt
- P0CD12
- Pockets
- 3 · best druggability 0.48
Structure
1 distinct chain · 79% helix, 2% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | NAD(P)H-quinone oxidoreductase subunit 2 a, chloroplastic | protein | 510 | 79% helix, 2% strand | P0CD12 |
Pockets
3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 148 | 0.48 | 0.77 | 21 | empty |
| 2 | 125 | 0.46 | 0.78 | 20 | empty |
| 3 | 74 | 0.32 | 0.73 | 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 P0CD12
- Elsewhere: UniProt P0CD12 · AlphaFold DB P0CD12
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