Lys210 participates in H-bond interactions (green) with the backbone carbonyls of Leu179 & Trp225 and a salt-bridge (orange) with Glu181. The glutaryl Co-A substrate is in the foreground.
Glutaryl-CoA dehydrogenase (GCDH)
Glutary CoA Dehydrogenase (GCDH) - Interactive
Closeup of symmetrical intra- and inter-molecular salt-bridges formed between Lys377 and Glu342, with H-bonds to Asn373.
View of the symmetrical salt-bridges from the opposite side
GCDH Ribbons
GCDH - Opaque Surface
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. All renders and baking of the high poly surface were done in Marmoset. Explicit solvent-based energy minimization of the crystal structure for human GCDH (PDB accession code 1SIR) provided the basis of the model.
