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Figure 3
The catalytic triad in the active site. (a) The superposed architecture of the catalytic triad in LmPTR1 structures in complex with substrates: folate (FOL; green sticks), biopterin (BIO; PDB entry 2bf7; blue sticks) and dihydrobiopterin (DHB; PDB entry 1e92; pink sticks). A black arrow indicates the anomalous distance between Tyr194 and Asp181 detected in our structure with folate compared with other substrates. (b) The superposed architecture of the catalytic triad in LmPTR1 (green) and TbPTR1 (pink; PDB entry 3bmc) structures in complex with folate. In both structures the Asp–Tyr distance in the triad is 3.8 Å. This figure was generated using PyMOL.

Journal logoSTRUCTURAL BIOLOGY
COMMUNICATIONS
ISSN: 2053-230X
Volume 78| Part 4| April 2022| Pages 170-176
https://doi.org/10.1107/S2053230X22002795
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