3KEG
X-ray Crystallographic Structure of a Y131F mutant of Pseudomonas Aeruginosa Azoreductase in complex with Methyl RED
Summary for 3KEG
| Entry DOI | 10.2210/pdb3keg/pdb |
| Descriptor | FMN-dependent NADH-azoreductase 1, FLAVIN MONONUCLEOTIDE, 2-(4-DIMETHYLAMINOPHENYL)DIAZENYLBENZOIC ACID, ... (5 entities in total) |
| Functional Keywords | y131f azoreductase, methyl red, flavoprotein, fmn, nad, oxidoreductase |
| Biological source | Pseudomonas aeruginosa |
| Total number of polymer chains | 2 |
| Total formula weight | 47665.53 |
| Authors | Wang, C.-J.,Laurieri, N.,Abuhammad, A.,Lowe, E.,Westwood, I.,Ryan, A.,Sim, E. (deposition date: 2009-10-26, release date: 2010-01-12, Last modification date: 2023-11-01) |
| Primary citation | Wang, C.-J.,Laurieri, N.,Abuhammad, A.,Lowe, E.,Westwood, I.,Ryan, A.,Sim, E. Role of tyrosine 131 in the active site of paAzoR1, an azoreductase with specificity for the inflammatory bowel disease prodrug balsalazide Acta Crystallogr.,Sect.F, 66:2-7, 2010 Cited by PubMed Abstract: Azoreductase 1 from Pseudomonas aeruginosa strain PAO1 (paAzoR1) catalyses the activation of the prodrug balsalazide and reduces the azo dye methyl red using reduced nicotinamide adenine dinucleotide cofactor as an electron donor. To investigate the mechanism of the enzyme, a Y131F mutation was introduced and the enzymic properties of the mutant were compared with those of the wild-type enzyme. The crystallographic structure of the mutant with methyl red bound was solved at 2.1 A resolution and compared with the wild-type structure. Tyr131 is important in the architecture of the active site but is not essential for enzymic activity. PubMed: 20057057DOI: 10.1107/S1744309109044741 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.1 Å) |
Structure validation
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