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EC Number Title Organism
Display the word mapDisplay the reaction diagram Show all sequences 7.2.2.6 Cryo-EM structures of KdpFABC suggest a K+ transport mechanism via two inter-subunit half-channels Escherichia coli
Display the word mapDisplay the reaction diagram Show all sequences 7.2.2.6 Regulation of potassium dependent ATPase (kdp) operon of Deinococcus radiodurans Deinococcus radiodurans
Display the word mapDisplay the reaction diagram Show all sequences 7.2.2.6 Regulation of potassium dependent ATPase (kdp) operon of Deinococcus radiodurans Deinococcus radiodurans DSM 20539
Display the word mapDisplay the reaction diagram Show all sequences 7.2.2.6Analysis of KdpC of the K+ -transporting KdpFABC complex of Escherichia coli Escherichia coli
Display the word mapDisplay the reaction diagram Show all sequences 7.2.2.6ATP binding properties of the soluble part of the KdpC subunit from the Escherichia coli K(+)-transporting KdpFABC P-type ATPase Escherichia coli
Display the word mapDisplay the reaction diagram Show all sequences 7.2.2.6ATP-driven potassium transport in right-side-out membrane vesicles via the Kdp system of Escherichia coli Escherichia coli
Display the word mapDisplay the reaction diagram Show all sequences 7.2.2.6ATP-driven potassium transport in right-side-out membrane vesicles via the Kdp system of Escherichia coli Escherichia coli TKA 1000
Display the word mapDisplay the reaction diagram Show all sequences 7.2.2.6Characterization of the phosphorylated intermediate of the K+-translocating Kdp-ATPase from Escherichia coli Escherichia coli
Display the word mapDisplay the reaction diagram Show all sequences 7.2.2.6Characterization of the phosphorylated intermediate of the K+-translocating Kdp-ATPase from Escherichia coli Escherichia coli TKA 1000
Display the word mapDisplay the reaction diagram Show all sequences 7.2.2.6Does the KdpA subunit from the high affinity K+-translocating P-type KDP-ATPase have a structure similar to that of K+ channels? Mycobacterium tuberculosis
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