5hpg
From Proteopedia
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STRUCTURE AND LIGAND DETERMINANTS OF THE RECOMBINANT KRINGLE 5 DOMAIN OF HUMAN PLASMINOGEN
Overview
The X-ray crystal structure of the recombinant (r) kringle 5 domain of, human plasminogen (K5HPg) has been solved by molecular replacement methods, using K1HPg as a model and refined at 1.7 A resolution to an R factor of, 16.6%. The asymmetric unit of K5HPg is composed of two molecules related, by a noncrystallographic 2-fold rotation axis approximately parallel to, the z-direction. The lysine binding site (LBS) is defined by the regions, His33-Thr37, Pro54-Val58, Pro61-Tyr64, and Leu71-Tyr74 and is occupied in, the apo-form by water molecules. A unique feature of the LBS of apo-K5HPg, is the substitution by Leu71 for the basic amino acid, arginine, that in, other kringle polypeptides forms the donor cationic center for the, carboxylate group of omega-amino acid ligands. While wild-type ... [(full description)]
About this Structure
5HPG is a [Single protein] structure of sequence from [Homo sapiens]. Active as [[1]], with EC number [3.4.21.7]. Full crystallographic information is available from [OCA].
Reference
Structure and ligand binding determinants of the recombinant kringle 5 domain of human plasminogen., Chang Y, Mochalkin I, McCance SG, Cheng B, Tulinsky A, Castellino FJ, Biochemistry. 1998 Mar 10;37(10):3258-71. PMID:9521645
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