2ACU
TYROSINE-48 IS THE PROTON DONOR AND HISTIDINE-110 DIRECTS SUBSTRATE STEREOCHEMICAL SELECTIVITY IN THE REDUCTION REACTION OF HUMAN ALDOSE REDUCTASE: ENZYME KINETICS AND THE CRYSTAL STRUCTURE OF THE Y48H MUTANT ENZYME
Summary for 2ACU
Entry DOI | 10.2210/pdb2acu/pdb |
Descriptor | ALDOSE REDUCTASE, NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE, CITRIC ACID, ... (4 entities in total) |
Functional Keywords | oxidoreductase |
Biological source | Homo sapiens (human) |
Cellular location | Cytoplasm: P15121 |
Total number of polymer chains | 1 |
Total formula weight | 36677.65 |
Authors | Bohren, K.M.,Grimshaw, C.E.,Lai, C.-J.,Gabbay, K.H.,Petsko, G.A.,Harrison, D.H.,Ringe, D. (deposition date: 1994-04-15, release date: 1994-07-31, Last modification date: 2024-02-14) |
Primary citation | Bohren, K.M.,Grimshaw, C.E.,Lai, C.J.,Harrison, D.H.,Ringe, D.,Petsko, G.A.,Gabbay, K.H. Tyrosine-48 is the proton donor and histidine-110 directs substrate stereochemical selectivity in the reduction reaction of human aldose reductase: enzyme kinetics and crystal structure of the Y48H mutant enzyme. Biochemistry, 33:2021-2032, 1994 Cited by PubMed: 8117659DOI: 10.1021/bi00174a007 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.76 Å) |
Structure validation
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