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. 1999 Feb 1;113(2):347–358. doi: 10.1085/jgp.113.2.347

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A mutation at position 463 in S6 affects the affinity of an ion binding site in the pore. Crystal structure of a region of the Streptomyces lividans prokaryotic potassium channel highlighting the S6 methionine and P-region valine interaction. (A) A side view of the interacting side chains (boxed region) within a single subunit. The GYG amino acids are labeled for easier orientation. (B) Top view of the methionine:valine interaction with all four subunits shown. The backbone carbonyl of the signature sequence valine stabilizes a potassium ion at its binding site in the ion conducting pore.