Sandbox 33: Difference between revisions

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The active site is where the substrate binds to the enzyme to be catalyzed. The ligand binds to the LIGAND CONTACTS of the protein.  There are mostly hydophilic residue in the active site because water enter the active site.  As previously mentioned, there are some hydrophobic interactions in the active site, which interacts with the hydrophobic portions of the substrate (or more likely, the transition state) to stabilize it during catalysis.  There are SIX CATALYTIC RESIDUES which are highlighted in COLOR which help perform the catalysis by forming hydrogen bonds with the substrate to hold it in place for the reaction.  The catalytic residues are all charged residues, including lysin, aspartic acid, and arginine.  These residues also allow for electrostatic interactions but can be effected by water in the active site.
The active site is where the substrate binds to the enzyme to be catalyzed. The ligand binds to the LIGAND CONTACTS of the protein.  There are mostly hydophilic residue in the active site because water enter the active site.  As previously mentioned, there are some hydrophobic interactions in the active site, which interacts with the hydrophobic portions of the substrate (or more likely, the transition state) to stabilize it during catalysis.  There are SIX CATALYTIC RESIDUES which are highlighted in COLOR which help perform the catalysis by forming hydrogen bonds with the substrate to hold it in place for the reaction.  The catalytic residues are all charged residues, including lysin, aspartic acid, and arginine.  These residues also allow for electrostatic interactions but can be effected by water in the active site.
==Resources==
http://en.wikipedia.org/wiki/Adenylate_kinase