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: 8117659 DOI: 10.1021/bi00174a007 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (1.76 Å)

Structure validation