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Figure 5
Description of the OPRTase obligate dimer. (a) Two subunits contribute to each of the two active sites of the PfOPRTase dimer. The two views, 180° apart, represent the surfaces of the two protomers (colored blue and green) of the PfOPRTase dimer with a large buried surface area of 1500 Å. The substrate-binding site on one face of the dimer is colored yellow. (b) The catalytic dimer of PfOPRTase is held together primarily by interprotomer hydrogen bonds, with contributions from one protomer shown in dark green and those from the other in light green.

Journal logoSTRUCTURAL BIOLOGY
COMMUNICATIONS
ISSN: 2053-230X
Volume 71| Part 5| April 2015| Pages 600-608
doi:10.1107/S2053230X1500549X
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