Sandbox 31: Difference between revisions
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==Structure== | ==Structure== | ||
The <scene name='Sandbox_31/Ak_secondary_structure/1'>secondary structure</scene> of adenylate kinase shows alpha | The <scene name='Sandbox_31/Ak_secondary_structure/1'>secondary structure</scene> of adenylate kinase shows alpha helices (cyan) and beta sheets (green) surrounding the non-hydrolysable substrate analogue (orange). Adenylate kinase has a <scene name='Sandbox_31/Ak_hydrophilic/1'>hydrophilic</scene> exterior, and a <scene name='Sandbox_31/Ak_hydrophobic/1'>hydrophobic</scene> core, with additional | ||
<scene name='Sandbox_31/Ak_hydrophilic_hydrophobic/1'>hydrophilic residues</scene> on the interior contacting the ligand. | <scene name='Sandbox_31/Ak_hydrophilic_hydrophobic/1'>hydrophilic residues</scene> on the interior contacting the ligand. | ||
Revision as of 17:00, 8 August 2012
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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 helices (cyan) and beta sheets (green) surrounding the non-hydrolysable 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 |