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AlphaFold monomer V2.0 prediction for glutamine-dependent NAD(+) synthetase (P9WJJ2)

Analyse AlphaFold monomer V2.0 prediction for glutamine-dependent NAD(+) synthetase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

Accession: P9WJJ2
Type: protein
Length: 679 residues
Chains: 1
Collection: MolNFT v1 / AlphaFold
Contract: 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
Owner: 0x9e5E98E011361C5888c92e2CDb7652E02Bd5C7Ed
Molecule: Glutamine-dependent NAD(+) synthetase
UniProt: P9WJJ2
Pockets: 7 · best druggability 0.82

Structure

1 distinct chain · 43% helix, 17% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Glutamine-dependent NAD(+) synthetase	protein	679	43% helix, 17% strand	P9WJJ2

Pockets

7 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	892	0.82	0.84	72	empty
2	424	0.69	0.81	35	empty
3	78	0.53	0.85	18	empty
4	60	0.40	0.81	15	empty
5	82	0.39	0.77	17	empty

Compared structures

6OFC · Crystal structure of M. tuberculosis glutamine-dependent NAD+ synthetase complexed with… · an experimental structure of the same protein · chain A against C, TM-score 0.98
6OFC · Crystal structure of M. tuberculosis glutamine-dependent NAD+ synthetase complexed with… · an experimental structure of the same protein · chain A against C, TM-score 0.98

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 P9WJJ2
Elsewhere: UniProt P9WJJ2 · AlphaFold DB P9WJJ2

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