Sandbox Reserved 1456: Difference between revisions

← Older edit Newer edit →

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA, Emily Albertsen

Revision as of 07:41, 17 November 2018 view source Emily Albertsen (talk \| contribs) 44 edits No edit summary ← Older edit		Revision as of 07:43, 17 November 2018 view source Emily Albertsen (talk \| contribs) 44 edits No edit summary Newer edit →
Line 18:		Line 18:


	The <scene name='79/799584/~~Ligand_ckc~~/1'>ligand</scene> of this molecule is		The <scene name='79/799584/Ligand_ckc_2/1'>ligand</scene> of this molecule is

	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.