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OCA, Emily Albertsen

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	The <scene name='79/799584/Ligand_2/1'>ligand</scene> of this molecule is (3S)-3,7-diaminoheptan-2-one, referred to as CKC. CKC has the same structure as lysine, having two protonated amine groups and a carboxylic acid group all capable of hydrogen bonding. The side chain of CKC contains four carbon groups which allows for a hydrophobic interaction. This molecule hydrogen bonds with the three amino acids of the catalytic triad to stabilize the structure of Kgp. The structure of the complex is maintained by hydrogen bond formation and a hydrophobic interaction with Trp513, thus decreasing entropy of the system and producing a favorable complex.		The <scene name='79/799584/Ligand_2/1'>ligand</scene> of this molecule is (3S)-3,7-diaminoheptan-2-one, referred to as CKC. CKC has the same structure as lysine, having two protonated amine groups and a carboxylic acid group all capable of hydrogen bonding. The side chain of CKC contains four carbon groups which allows for a hydrophobic interaction. This molecule hydrogen bonds with the three amino acids of the catalytic triad to stabilize the structure of Kgp. The structure of the complex is maintained by hydrogen bond formation and a hydrophobic interaction with Trp513, thus decreasing entropy of the system and producing a favorable complex. [[image:catalytic_triad.pdf]]

	The <scene name='79/799584/Catalytic_triad/1'>catalytic triad</scene> of Kgp is made up of Cys477-His444-Asp388. The ligand, CKC, is shown in red and the three amino acids of the catalytic triad are colored by elements (CPK). His444 and Asp388 use acid base catalysis with a covalent intermediate formed with Cys477 to cleave the peptide bond. The histidine imidazolium group transfers a proton to the leaving alpha-amine group of the cleavage product, leaving part of the substrate bound covalently as a thioester to the catalytic Cys477.		The <scene name='79/799584/Catalytic_triad/1'>catalytic triad</scene> of Kgp is made up of Cys477-His444-Asp388. The ligand, CKC, is shown in red and the three amino acids of the catalytic triad are colored by elements (CPK). His444 and Asp388 use acid base catalysis with a covalent intermediate formed with Cys477 to cleave the peptide bond. The histidine imidazolium group transfers a proton to the leaving alpha-amine group of the cleavage product, leaving part of the substrate bound covalently as a thioester to the catalytic Cys477.