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. 2023 Jun 21;24(13):10464. doi: 10.3390/ijms241310464

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© 2023 by the authors.

Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/).

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Projection of water occupancy in the D-channel of CcO for varying D-channel protonation. The different models are labelled according to the protonation states of residues D132, E286, K362, and E101, where “0” means unprotonated and “1” means protonated (see Table 5 in “Materials and Methods”). (For the projections of all models, see Supplementary Figure S42.) In the K-channel, K362 is protonated (*10 models). The lower row shows a view 90 degrees rotated from that of the upper row. The symbols mark the average height of protein residues H26 (dark blue rectangle ), N121 (cyan arrow—left ), D132 (lime diamond ), N139 (purple arrow—right ), and E286 (orange star ). Residues with an excess proton are marked by a grey circle around the symbols representing the respective residues.

Inline graphic — Projection of water occupancy in the D-channel of CcO for varying D-channel protonation. The different models are labelled according to the protonation states of residues D132, E286, K362, and E101, where “0” means unprotonated and “1” means protonated (see Table 5 in “Materials and Methods”). (For the projections of all models, see Supplementary Figure S42.) In the K-channel, K362 is protonated (*10 models). The lower row shows a view 90 degrees rotated from that of the upper row. The symbols mark the average height of protein residues H26 (dark blue rectangle ), N121 (cyan arrow—left ), D132 (lime diamond ), N139 (purple arrow—right ), and E286 (orange star ). Residues with an excess proton are marked by a grey circle around the symbols representing the respective residues.