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AlphaFold monomer V2.0 prediction for NAD(P)H-quinone oxidoreductase subunit N, chloroplastic (Q9LVM2)

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

Accession: Q9LVM2
Type: protein
Length: 209 residues
Chains: 1
Collection: MolNFT v1 / AlphaFold
Contract: 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
Owner: 0x665CBc036828f0545913b4B24EA0229BB1e4F3f2
Molecule: NAD(P)H-quinone oxidoreductase subunit N, chloroplastic
UniProt: Q9LVM2
Pockets: 1 · best druggability 0.37

Structure

1 distinct chain · 31% helix, 20% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	NAD(P)H-quinone oxidoreductase subunit N, chloroplastic	protein	209	31% helix, 20% strand	Q9LVM2

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	70	0.37	0.78	13	empty

Compared structures

7WG5 · Cyclic electron transport supercomplex NDH-PSI from Arabidopsis · an experimental structure of the same protein · chain A against N, TM-score 0.64
7WFG · Subcomplexes a and E in ndh complex from arabidopsis · an experimental structure of the same protein · chain A against N, TM-score 0.64
7WFG · Subcomplexes A and E in NDH complex from Arabidopsis · an experimental structure of the same protein · chain A against N, TM-score 0.64

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 Q9LVM2
Elsewhere: UniProt Q9LVM2 · AlphaFold DB Q9LVM2

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