Sandbox 31: Difference between revisions
No edit summary |
No edit summary |
||
| Line 29: | Line 29: | ||
together you can see that the <scene name='Sandbox_31/Ak_ligand_binding_and_active_s/1'>active site</scene> is only a fraction of the molecules involved in binding the ligand. | together you can see that the <scene name='Sandbox_31/Ak_ligand_binding_and_active_s/1'>active site</scene> is only a fraction of the molecules involved in binding the ligand. | ||
<Structure load='3be4' size='500' frame='true' align='right' caption='Cryptosporidium parvum' scene='adenylate kinase' /> | |||
Comparing the E.coli structure to <scene name='Sandbox_31/Ak_cryptosporidium_parvum/1'>Cryptosporidium parvum</scene> | |||
==References== | ==References== | ||
<references/> | <references/> | ||
Revision as of 14:21, 8 August 2012
>
Please do NOT make changes to this Sandbox. Sandboxes 30-60 are reserved for use by Biochemistry 410 & 412 at Messiah College taught by Dr. Hannah Tims during Fall 2012 and Spring 2013.
Adenylate Kinase (PDB ID #: 1ake)
IntroductionAdenylate Kinase is a good little protein.
Physical PropertiesAdenylate kinase is caged with water molecules. StructureThe secondary structure of adenylate kinase shows alpha helicies (cyan) and beta sheets (green) surrounding the non-hydrolyzable substrate analogue (orange). Adenylate kinase has a hydrophilic exterior, and a hydrophobic core, with additional hydrophilic residues on the interior contacting the ligand. Active Site and Mechanismresidues within 3 angstroms of the ligand are involved in binding the ligand or stabilizing the active site. adenylate kinase's active site is highlighted in dark blue. together you can see that the active site is only a fraction of the molecules involved in binding the ligand.
Comparing the E.coli structure to Cryptosporidium parvum References |