Research workbench
AlphaFold monomer V2.0 prediction for NAD(P)H-quinone oxidoreductase subunit M, chloroplastic (Q2V2S7)
Analyse AlphaFold monomer V2.0 prediction for NAD(P)H-quinone oxidoreductase subunit M… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q2V2S7
- Type
- protein
- Length
- 217 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x0B240F978546CA1A04E3ff43f85651dF169A524D
- Molecule
- NAD(P)H-quinone oxidoreductase subunit M, chloroplastic
- UniProt
- Q2V2S7
- Pockets
- 2 · best druggability 0.53
Structure
1 distinct chain · 20% helix, 12% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | NAD(P)H-quinone oxidoreductase subunit M, chloroplastic | protein | 217 | 20% helix, 12% strand | Q2V2S7 |
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 143 | 0.53 | 0.81 | 19 | empty |
| 2 | 77 | 0.37 | 0.77 | 18 | empty |
Compared structures
- 7WFG · Subcomplexes a and E in ndh complex from arabidopsis · an experimental structure of the same protein · chain A against M, TM-score 0.48
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 Q2V2S7
- Elsewhere: UniProt Q2V2S7 · AlphaFold DB Q2V2S7
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