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. 2005 Oct 7;102(42):14994–14999. doi: 10.1073/pnas.0506254102

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Copyright © 2005, The National Academy of Sciences

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Fig. 4. — Ammonium recruitment site and substrate channel. presumably forms a hydrogen bond to the side chain of S208 on the extracellular side of Amt-1 (at the top), stabilized by a π interaction with the side chain of W137. The hydrophobic channel leading to the cytoplasmic side is blocked by F96 and F204, with the latter having significantly elevated B factors, an indication of structural flexibility. The N_δ atoms of two conserved histidine residues, H157 and H305, are in hydrogen-bonding distance and their imidazole rings are almost perfectly coplanar.

Inline graphic — Ammonium recruitment site and substrate channel. presumably forms a hydrogen bond to the side chain of S208 on the extracellular side of Amt-1 (at the top), stabilized by a π interaction with the side chain of W137. The hydrophobic channel leading to the cytoplasmic side is blocked by F96 and F204, with the latter having significantly elevated B factors, an indication of structural flexibility. The N_δ atoms of two conserved histidine residues, H157 and H305, are in hydrogen-bonding distance and their imidazole rings are almost perfectly coplanar.