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AlphaFold monomer V2.0 prediction for NAD(P)H-quinone oxidoreductase subunit 1, chloroplastic (P92432)

Analyse AlphaFold monomer V2.0 prediction for NAD(P)H-quinone oxidoreductase subunit 1… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

Accession: P92432
Type: protein
Length: 362 residues
Chains: 1
Collection: MolNFT v1 / AlphaFold
Contract: 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
Owner: 0x3a0681B8E5eC7273ad7d9f8fD7D4103724E97da7
Molecule: NAD(P)H-quinone oxidoreductase subunit 1, chloroplastic
UniProt: P92432
Pockets: 4 · best druggability 0.73

Structure

1 distinct chain · 74% helix, 1% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	NAD(P)H-quinone oxidoreductase subunit 1, chloroplastic	protein	362	74% helix, 1% strand	P92432

Pockets

4 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	70	0.73	0.98	23	empty
2	310	0.58	0.77	38	empty
3	93	0.52	0.82	15	empty
4	88	0.33	0.73	15	empty

Compared structures

7EU3 · Chloroplast ndh complex · an experimental structure of the same protein · chain A against A, TM-score 0.90
7F9O · PSI-NDH supercomplex of Barley · an experimental structure of the same protein · chain A against G, TM-score 0.90
7EU3 · Chloroplast NDH complex · an experimental structure of the same protein · chain A against A, TM-score 0.90

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 P92432
Elsewhere: UniProt P92432 · AlphaFold DB P92432

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