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AlphaFold monomer V2.0 prediction for NADH-quinone oxidoreductase subunit D (A0QU33)

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

Accession: A0QU33
Type: protein
Length: 442 residues
Chains: 1
Collection: MolNFT v1 / AlphaFold
Contract: 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
Owner: 0x738c1929c69B751bD0Be0B962D9bac20B631aAc6
Molecule: NADH-quinone oxidoreductase subunit D
UniProt: A0QU33
Pockets: 5 · best druggability 0.67

Structure

1 distinct chain · 50% helix, 13% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	NADH-quinone oxidoreductase subunit D	protein	442	50% helix, 13% strand	A0QU33

Pockets

5 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	50	0.67	0.97	17	empty
2	91	0.56	0.86	23	empty
3	134	0.40	0.74	24	empty
4	89	0.35	0.75	23	empty
5	83	0.32	0.73	22	empty

Compared structures

8E9H · Mycobacterial respiratory complex I, fully-inserted qui · an experimental structure of the same protein · chain A against D, TM-score 0.91
8E9I · Mycobacterial respiratory complex I, semi-inserted qui · an experimental structure of the same protein · chain A against D, TM-score 0.91
8E9G · Mycobacterial respiratory complex I with both qui positions modelled · an experimental structure of the same protein · chain A against D, TM-score 0.91

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 A0QU33
Elsewhere: UniProt A0QU33 · AlphaFold DB A0QU33

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