PTM Locations on Glutaryl CoA Dehydrogenase (GCDH)
Global view with surfaces

Global view with surfaces

Lys210 is located in close proximity to the substrate and cofactor binding sites

Lys210 is located in close proximity to the substrate and cofactor binding sites

Closeup of symmetrical intra- and inter-molecular salt-bridges formed between Lys377 and Glu342 on opposing monomers, with H-bonds to Asn373.

Closeup of symmetrical intra- and inter-molecular salt-bridges formed between Lys377 and Glu342 on opposing monomers, with H-bonds to Asn373.

Intramolecular Lysine Interactions

Intramolecular Lysine Interactions

Interactive GCDH with surfaces

Interactive GCDH - ribbons only

Human Glutaryl CoA Dehydrogenase (GCDH)

Final Manuscript Figure 1

Final Manuscript Figure 1

Final Manuscript Figure 2

Final Manuscript Figure 2

Global View - rotated 90 degrees

Global View - rotated 90 degrees

PTM Locations on Glutaryl CoA Dehydrogenase (GCDH)

Glutaryl-CoA-dehydrogenase (GCDH) is a homotetrameric enzyme that catalyzes the conversion of glutaryl-CoA to crotonyl-CoA as part of the L-lysine and L-tryptophan metabolic pathway. Each monomer of the enzyme is rendered in a different color.
Lysine residues in monomer 4 (purple) that are subject to post-translational modification are highlighted in yellow and most of these appear to have important roles in the normal function of the protein. Hydrogen bonds are colored green and salt-bridge/electrostatic interactions are colored orange. Baking of the high poly surface was done in Marmoset. Renders were done in Marmoset except for those in the final published manuscript version, which were done in Lightwave 2018. Explicit solvent-based energy minimization of the crystal structure for human GCDH (PDB accession code 1SIR) provided the basis of the model.

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