Summary for 2ALR
| Entry DOI | 10.2210/pdb2alr/pdb |
| Descriptor | ALDEHYDE REDUCTASE (1 entity in total) |
| Functional Keywords | oxidoreductase, tim-barrel |
| Biological source | Homo sapiens (human) |
| Total number of polymer chains | 1 |
| Total formula weight | 36486.77 |
| Authors | El-Kabbani, O. (deposition date: 1994-09-06, release date: 1996-06-20, Last modification date: 2024-02-14) |
| Primary citation | El-Kabbani, O.,Green, N.C.,Lin, G.,Carson, M.,Narayana, S.V.,Moore, K.M.,Flynn, T.G.,DeLucas, L.J. Structures of human and porcine aldehyde reductase: an enzyme implicated in diabetic complications. Acta Crystallogr.,Sect.D, 50:859-868, 1994 Cited by PubMed Abstract: The crystal structures of porcine and human aldehyde reductase, an enzyme implicated in complications of diabetes, have been determined by X-ray diffraction methods. The crystallographic R factor for the refined porcine aldehyde reductase model is 0.19 at 2.8 A resolution. There are two molecules in the asymmetric unit related by a local non-crystallographic twofold axis. The human aldehyde reductase model has been refined to an R factor of 0.21 at 2.48 A resolution. The amino-acid sequence of porcine aldehyde reductase revealed a remarkable homology with human aldehyde reductase. The coenzyme-binding site residues are conserved and adopt similar conformations in human and porcine aldehyde reductase apo-enzymes. The tertiary structures of aldhyde reductase and aldose reductase are similar and consist of a beta/alpha-barrel, with the coenzyme-binding site located at the carboxy-terminus end of the strands of the barrel. The crystal structure of porcine and human aldehyde reductase should allow in vitro mutagenesis to elucidate the mechanism of action for this enzyme and facilitate the effective design of specific inhibitors. PubMed: 15299353DOI: 10.1107/S0907444994005275 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.48 Å) |
Structure validation
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