3O3R
Crystal Structure of AKR1B14 in complex with NADP
Summary for 3O3R
| Entry DOI | 10.2210/pdb3o3r/pdb |
| Descriptor | Aldo-keto reductase family 1, member B7, NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE (3 entities in total) |
| Functional Keywords | aldose reductase like protein, akr1b14, oxidoreductase |
| Biological source | Rattus norvegicus (Rat) |
| Total number of polymer chains | 2 |
| Total formula weight | 73834.33 |
| Authors | Sundaram, K.,Dhagat, U.,El-Kabbani, O. (deposition date: 2010-07-26, release date: 2011-01-19, Last modification date: 2023-11-01) |
| Primary citation | Sundaram, K.,Dhagat, U.,Endo, S.,Chung, R.,Matsunaga, T.,Hara, A.,El-Kabbani, O. Structure of rat aldose reductase-like protein AKR1B14 holoenzyme: Probing the role of His269 in coenzyme binding by site-directed mutagenesis Bioorg.Med.Chem.Lett., 21:801-804, 2011 Cited by PubMed Abstract: Rat aldose reductase-like protein (AKR1B14) is the ortholog of mouse vas deferens protein (AKR1B7) playing roles in detoxification of reactive aldehydes and synthesis of prostaglandin F(2α). The crystal structure of the binary complex (AKR1B14-NADPH) was determined at 1.86Å resolution, and showed that the adenine ring and the 2'-phosphate group of the coenzyme formed π-stacking and electrostatic interactions with the imidazole ring and ND1 atom, respectively, of His269, which is not conserved in other aldose reductase-like proteins. The interactions were supported by site-directed mutagenesis of His269 to Arg, Phe and Met, which increased the K(m) for NADPH by 4, 7 and 127-fold, respectively. This is the first report of the tertiary structure of a rodent AKR1B7 ortholog, which describes the role of a novel dual interaction for the non-conserved His269 in coenzyme binding. PubMed: 21168333DOI: 10.1016/j.bmcl.2010.11.086 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.86 Å) |
Structure validation
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