Succinyl-CoA synthetase
From Proteopedia
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<applet load='1cqj' size='300' frame='true' align='right' caption='Structure of succinyl-CoA synthetase' /> | <applet load='1cqj' size='300' frame='true' align='right' caption='Structure of succinyl-CoA synthetase' /> | ||
| - | '''Succinyl-Coa synthetase''' catalyzes the reversible reaction of succinyl-CoA + | + | '''Succinyl-Coa synthetase''' catalyzes the reversible reaction of succinyl-CoA + NDP + Pi <-> succinate + CoA + NTP (where N is either adenosine or guanosine. |
==Structure== | ==Structure== | ||
| - | '''Succinyl-CoA synthetase''' is a tetramer with an active site on each dimer. This can be seen in the Jmol representation (the PDB code is 1CQJ). | + | '''Succinyl-CoA synthetase''' is a tetramer with an active site on each dimer. This can be seen in the Jmol representation (the PDB code is 1CQJ). The two dimers are denoted alpha and beta with a Histidine residue (His 246 alpha) being the primary catalysis through a phosphorylated histidine intermediate. |
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| + | <scene name='Lucas_Hamlow_sandbox_1/Active_sites/1'>The Histidine 246 Residues active in catalysis.</scene> | ||
Revision as of 08:31, 28 February 2010
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Succinyl-Coa synthetase catalyzes the reversible reaction of succinyl-CoA + NDP + Pi <-> succinate + CoA + NTP (where N is either adenosine or guanosine.
Structure
Succinyl-CoA synthetase is a tetramer with an active site on each dimer. This can be seen in the Jmol representation (the PDB code is 1CQJ). The two dimers are denoted alpha and beta with a Histidine residue (His 246 alpha) being the primary catalysis through a phosphorylated histidine intermediate.
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.
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Proteopedia Page Contributors and Editors (what is this?)
Michal Harel, Lucas Hamlow, J.D. McClintic, Wayne Decatur, David Canner, Alexander Berchansky
