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AlphaFold monomer V2.0 prediction for trifunctional NAD BIOSYNTHESIS/REGULATOR protein nadr (P27278)

Analyse AlphaFold monomer V2.0 prediction for trifunctional NAD BIOSYNTHESIS/REGULATOR… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

Accession: P27278
Type: protein
Length: 410 residues
Chains: 1
Collection: MolNFT v1 / AlphaFold
Contract: 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
Owner: 0x9F605311B7e26e76340423EfAfbE5e2EFc7A0b7C
Molecule: Trifunctional NAD BIOSYNTHESIS/REGULATOR protein nadr
UniProt: P27278
Pockets: 4 · best druggability 0.73

Structure

1 distinct chain · 48% helix, 12% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Trifunctional NAD BIOSYNTHESIS/REGULATOR protein nadr	protein	410	48% helix, 12% strand	P27278

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	76	0.73	0.97	19	empty
2	396	0.71	0.82	41	empty
3	234	0.50	0.75	22	empty
4	138	0.37	0.72	19	empty

Compared structures

8X7F · CryoEM structure of the trifunctional NAD biosynthesis/regulator protein NadR in complex… · an experimental structure of the same protein · chain A against D, TM-score 0.79

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 P27278
Elsewhere: UniProt P27278 · AlphaFold DB P27278

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