Succinyl-CoA synthetase
From Proteopedia
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Succinyl-Coa synthetase catalyzes the reversible reaction of succinyl-CoA + ADP + Pi <-> succinate + CoA + ATP.
Structure
Succinyl-CoA synthetase
The B chain consists of . As is true for all of the "trypsin-like" serine proteases, each of the two thrombin domains consists mainly of a 6-stranded, antiparallel beta barrel. The specificity pocket (here filled with the Lys sidechain of the PPACK inhibitor) is in one side of the throat of the domain 2beta barrel, and the activation site is close next to it.
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Trypsin-BPTI complex
The trypsin backbone is shown in pink and the trypsin inhibitor, BPTI, in yellow (PDB code 2ptc). The residues [Ser195-His57-Asp102-Ser214] are shown in green, the disulfide bond between residues 14-38 is shown in yellow and the Lys 15 sidechain at the specificity site in pink.
Content Donators
- Content for this page has been included and adapted with permission from Jane S. and David C. Richardson's http://kinemage.biochem.duke.edu/
Proteopedia Page Contributors and Editors (what is this?)
Michal Harel, Lucas Hamlow, J.D. McClintic, Wayne Decatur, David Canner, Alexander Berchansky
