Sandbox Reserved 784

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<scene name='56/563196/Domains_h_bonds/2'>Hydrogen bonds</scene> in the backbone show the interactions within the elements of secondary structure.
<scene name='56/563196/Domains_h_bonds/2'>Hydrogen bonds</scene> in the backbone show the interactions within the elements of secondary structure.
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<scene name='56/563196/Hydrophobics/1'>only hydrophobics</scene>
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<scene name='56/563196/Charged/2'>Hydrophobicity</scene> of the side chains is shown. Hydrophobic side chains are grey while hydrophilic side chains are purple. You can see that the hydrophobic residues are mostly on the interior, buried within the protein, while hydrophilic are on the outside. <scene name='56/563196/Waters_one_chain/1'>Water</scene> is in contact with most of the chain except the <scene name='56/563196/Domains_water_one_chain/1'>domain</scene> 3 beta barrel (shown in green). When looking at the quaternary <scene name='56/563196/Waters_whole/1'>structure</scene>, water is present over most of the exterior except the cavity in the middle and the outer barrels in <scene name='56/563196/Domains_water_whole/1'>domain</scene> 3 (green).
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<scene name='56/563196/Charged/2'>charged and polar</scene>
 
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Solvent
 
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<scene name='56/563196/Waters_one_chain/1'>water on one chain</scene>
 
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When you look at <scene name='56/563196/Waters_whole/1'>water on the whole thing</scene>, you see that water surrounds everywhere except the
 
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<scene name='56/563196/Domains_water_one_chain/1'>domains one chain</scene>
 
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<scene name='56/563196/Domains_water_whole/1'>domains water whole</scene>
 
The ligands, substrate, cofactors, etc
The ligands, substrate, cofactors, etc

Revision as of 18:03, 18 October 2013

This Sandbox is Reserved from Oct 10, 2013, through May 20, 2014 for use in the course "CHEM 410 Biochemistry 1 and 2" taught by Hanna Tims at the Messiah College. This reservation includes Sandbox Reserved 780 through Sandbox Reserved 807.
To get started:
  • Click the edit this page tab at the top. Save the page after each step, then edit it again.
  • Click the 3D button (when editing, above the wikitext box) to insert Jmol.
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More help: Help:Editing

pyruvate kinase

Drag the structure with the mouse to rotate

Introduction

Pyruvate kinase (a transferase, PDB 4IP7) What's it do Research about it

Structure

Pyruvate kinase is a , meaning it has four identical . This enzyme contains both and .

It has three . consists of an alpha-beta-alpha 3-layer sandwich. consists of a parallel alpha-beta barrel. consists of an anti-parallel beta-barrel.

in the backbone show the interactions within the elements of secondary structure.

of the side chains is shown. Hydrophobic side chains are grey while hydrophilic side chains are purple. You can see that the hydrophobic residues are mostly on the interior, buried within the protein, while hydrophilic are on the outside. is in contact with most of the chain except the 3 beta barrel (shown in green). When looking at the quaternary , water is present over most of the exterior except the cavity in the middle and the outer barrels in 3 (green).


The ligands, substrate, cofactors, etc What kinds of side chains?


Ligand contacts


Catalytic residues

in green

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