File:Binding Site of Ubiquinone.JPG
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| Description |
English: Ubiquinone’s binding site is located in gap comprised of SdhB, SdhC, and SdhD. Ubiquinone is stabilized by the side chains of His207 of subunit B, Ser27 and Arg31C of subunit C, and Tyr83 of subunit D. These side chains are shown in grey. Nitrogens are blue and oxygens are red. Ubiquinone is shown in white and the heme group (aqua) is also shown. Tyr83 forms an additional hydrogen bond to Arg31 of subunit C, which allows a proton to directly translocate from the Tyr83 to ubiquinone when it is reduced. The quinone ring is surrounded by Ile28 of subunit C and Pro160 of subunit B. These residues, along with Ile209, Trp163, Trp164 of subunit B, and Ser27 of subunit C, form the hydrophobic environment of the quinone-binding pocket (not shown in the image). |
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| Date | |||
| Source | Adamandalex created this work entirely by himself/harself. The file was created from PDB: 2acz. | ||
| Author | Original uploader was Adamandalex at en.wikipedia | ||
| Permission (Reusing this file) |
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| Date/Time | Thumbnail | Dimensions | User | Comment | |
|---|---|---|---|---|---|
| current | 12:38, 7 April 2010 | | 1,280 × 625 (55 KB) | Akane700 | {{Information |Description={{en|1=Ubiquinone’s binding site is located in gap comprised of SdhB, SdhC, and SdhD. Ubiquinone is stabilized by the side chains of His207 of subunit B, Ser27 and Arg31C of subunit C, and Tyr83 of subunit D. These side chains |
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