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Literature summary extracted from

  • Devi, P.; Adhikari, S.
    Homology modeling and functional sites prediction of azoreductase enzyme from the cyanobacterium Nostoc sp. PCC7120 (2012), Interdiscip. Sci., 4, 310-318.
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.7.1.6 homology modeling and multiple sequence alignment shows conserved regions at different stretches from amino acid residues 1-11, 40-57, 82-120 and 161-177 Nostoc sp.

Organism

EC Number Organism UniProt Comment Textmining
1.7.1.6 Nostoc sp. Q8YV76
-
-
1.7.1.6 Nostoc sp. PCC 7120 Q8YV76
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-

Synonyms

EC Number Synonyms Comment Organism
1.7.1.6 NADH-azoreductase
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 Nostoc sp.

Cofactor

EC Number Cofactor Comment Organism Structure
1.7.1.6 FMN enzyme sequence consists of different sites such as FMN-dependent NADH-azoreductase site azoR, residues 2-204, flavodoxin-like fold, residues 2-205, NADPH-dependent FMN reductase, residues 2-205, cAMP and cGMP-dependent protein kinase phosphorylation site Nostoc sp.
1.7.1.6 NADH enzyme sequence consists of different sites such as FMN-dependent NADH-azoreductase site azoR, residues 2-204, flavodoxin-like fold, residues 2-205, NADPH-dependent FMN reductase, residues 2-205, cAMP and cGMP-dependent protein kinase phosphorylation site Nostoc sp.
1.7.1.6 NADPH enzyme sequence consists of different sites such as FMN-dependent NADH-azoreductase site azoR, residues 2-204, flavodoxin-like fold, residues 2-205, NADPH-dependent FMN reductase, residues 2-205, cAMP and cGMP-dependent protein kinase phosphorylation site Nostoc sp.