Research workbench
AlphaFold monomer V2.0 prediction for NAD(P)H-quinone oxidoreductase subunit 3, chloroplastic (P56751)
Analyse AlphaFold monomer V2.0 prediction for NAD(P)H-quinone oxidoreductase subunit 3… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P56751
- Type
- protein
- Length
- 120 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x78Cc7f9BF18AF8279e492D45EE7Fe9d7cC6f6D07
- Molecule
- NAD(P)H-quinone oxidoreductase subunit 3, chloroplastic
- UniProt
- P56751
Structure
1 distinct chain · 66% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | NAD(P)H-quinone oxidoreductase subunit 3, chloroplastic | protein | 120 | 66% helix, 0% strand | P56751 |
Compared structures
- 7WFF · Subcomplexes B,M and L in the cylic electron transfer supercomplex ndh-psi from… · an experimental structure of the same protein · chain A against C, TM-score 0.71
- 7WFF · Subcomplexes B,M and L in the Cylic electron transfer supercomplex NDH-PSI from… · an experimental structure of the same protein · chain A against C, TM-score 0.71
- 7WG5 · Cyclic electron transport supercomplex NDH-PSI from Arabidopsis · an experimental structure of the same protein · chain A against C, TM-score 0.70
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 P56751
- Elsewhere: UniProt P56751 · AlphaFold DB P56751
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