7F3Z

Double mutant Plasmodium falciparum dihydrofolate reductase-thymidylate synthase (PfDHFR-TS-K1, C59R+S108N) complexed with Trimethoprim (TOP), NADPH and dUMP

7F3Z の概要

• エントリーDOI: 10.2210/pdb7f3z/pdb
• 分子名称: Bifunctional dihydrofolate reductase-thymidylate synthase, NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE, 2'-DEOXYURIDINE 5'-MONOPHOSPHATE, ... (6 entities in total)
• 機能のキーワード: pfdhfr, trimethoprim, dihydrofolate reductase, plasmodium falciparum, structural protein
• 由来する生物種: Plasmodium falciparum
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 146690.19

構造登録者

Vanichtanankul, J.,Tanramluk, D.,Chitnumsub, P.,Yuvaniyama, J.,Yuthavong, Y. (登録日: 2021-06-17, 公開日: 2021-09-22, 最終更新日: 2023-11-29)

主引用文献

Tanramluk, D.,Pakotiprapha, D.,Phoochaijaroen, S.,Chantravisut, P.,Thampradid, S.,Vanichtanankul, J.,Narupiyakul, L.,Akavipat, R.,Yuvaniyama, J.
MANORAA: A machine learning platform to guide protein-ligand design by anchors and influential distances.
Structure, 30:181-189.e5, 2022

PubMed Abstract: The MANORAA platform uses structure-based approaches to provide information on drug design originally derived from mapping tens of thousands of amino acids on a grid. In-depth analyses of the pockets, frequently occurring atoms, influential distances, and active-site boundaries are used for the analysis of active sites. The algorithms derived provide model equations that can predict whether changes in distances, such as contraction or expansion, will result in improved binding affinity. The algorithm is confirmed using kinetic studies of dihydrofolate reductase (DHFR), together with two DHFR-TS crystal structures. Empirical analyses of 881 crystal structures involving 180 ligands are used to interpret protein-ligand binding affinities. MANORAA links to major biological databases for web-based analysis of drug design. The frequency of atoms inside the main protease structures, including those from SARS-CoV-2, shows how the rigid part of the ligand can be used as a probe for molecular design (http://manoraa.org).

PubMed: 34614393
DOI: 10.1016/j.str.2021.09.004

実験手法

X-RAY DIFFRACTION (2.6 Å)