Nitroreductase
From Proteopedia
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<StructureSection load='1icr' size='350' side='right' caption='E. coli nitroreductase dimer containing FMN and nicotinic acid (PDB entry [[1icr]])' scene=''> | <StructureSection load='1icr' size='350' side='right' caption='E. coli nitroreductase dimer containing FMN and nicotinic acid (PDB entry [[1icr]])' scene=''> | ||
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== Relevance == | == Relevance == | ||
| - | + | NR is of special interest due to its potential use as activator of prodrugs in cancer therapy. | |
== Structural highlights == | == Structural highlights == | ||
| + | NR cofactor FMN is bound to one subunit while the ligand - nicotinic acid - interacts with both subunits. | ||
</StructureSection> | </StructureSection> | ||
Revision as of 10:06, 15 May 2016
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3D structures of nitroreductase
Updated on 15-May-2016
References
- ↑ Lovering AL, Hyde EI, Searle PF, White SA. The structure of Escherichia coli nitroreductase complexed with nicotinic acid: three crystal forms at 1.7 A, 1.8 A and 2.4 A resolution. J Mol Biol. 2001 May 25;309(1):203-13. PMID:11491290 doi:10.1006/jmbi.2001.4653
