Sandbox Reserved 784
From Proteopedia
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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. | ||
| - | <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/ | + | <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_2/1'>Water</scene> is in contact with most of the chain except the largely hydrophobic <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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| + | The <scene name='56/563196/Interactions/1'>ligand FLC interacts</scene> with <scene name='56/563196/Interactions/2'>residues</scene> such as Arg (+ charge), Lys (+ charge), Thr (polar), Gly (nonpolar), and Asp (- charge). | ||
Catalytic residues | Catalytic residues | ||
| - | <scene name='56/563196/3gqy/1'>3GQY</scene> | + | The 4IP7 form of pyruvate kinase does not contain catalytic residues according to PDBsum. However, <scene name='56/563196/3gqy/1'>3GQY</scene>, the activator-bound form, shows similar |
| - | <scene name='56/563196/3gqy_ligand_interaction/ | + | <scene name='56/563196/3gqy_ligand_interaction/2'>ligand interactions</scene> and does show its <scene name='56/563196/3gqy_active_site/2'>active site</scene> (in green). |
| - | <scene name='56/563196/3gqy_active_site/ | + | |
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Revision as of 18:31, 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. |
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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 largely hydrophobic 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 with such as Arg (+ charge), Lys (+ charge), Thr (polar), Gly (nonpolar), and Asp (- charge).
Catalytic residues
The 4IP7 form of pyruvate kinase does not contain catalytic residues according to PDBsum. However, , the activator-bound form, shows similar and does show its (in green).
