Sandbox 35
From Proteopedia
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<scene name='Sandbox_35/2nd_struc_papain_helix/2'>alpha helix</scene> <ref name="9PAP PDB">[http://www.pdb.org/pdb/explore/explore.do?structureId=9PAP]9PAP PDB</ref> | <scene name='Sandbox_35/2nd_struc_papain_helix/2'>alpha helix</scene> <ref name="9PAP PDB">[http://www.pdb.org/pdb/explore/explore.do?structureId=9PAP]9PAP PDB</ref> | ||
| - | <scene name='Sandbox_35/Active_site_papain/3'>active site</scene> <ref | + | <scene name='Sandbox_35/Active_site_papain/3'>active site</scene> <ref>PMID: 8140097</ref> |
| + | |||
===Distribution of Residues=== | ===Distribution of Residues=== | ||
<scene name='Sandbox_35/Hydrophobic_papain/1'>non-polar and polar residues</scene> | <scene name='Sandbox_35/Hydrophobic_papain/1'>non-polar and polar residues</scene> | ||
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==Catalytic Mechanism== | ==Catalytic Mechanism== | ||
| + | [[Image:Papainmech6.jpg|200px|left|thumb| General mechanism of papain catalysis<ref>[http://chemistry.umeche.maine.edu/CHY431/Peptidase10.html] University of Maine</ref>.]] | ||
==References== | ==References== | ||
<references /> | <references /> | ||
| + | <ref group="xtra">PMID:8140097</ref><references group="xtra"/> | ||
| + | |||
http://www.pdb.org/pdb/explore/explore.do?structureId=2PAD | http://www.pdb.org/pdb/explore/explore.do?structureId=2PAD | ||
• Show the secondary structures. | • Show the secondary structures. | ||
Revision as of 03:16, 13 November 2011
| 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. |
Contents |
Papain
Introduction
finds its origin from the latex of the papaya fruit and is classified as a sulfhydryl protease.
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Catalytic Mechanism
References
- ↑ [1]9PAP PDB
- ↑ Wang J, Xiang YF, Lim C. The double catalytic triad, Cys25-His159-Asp158 and Cys25-His159-Asn175, in papain catalysis: role of Asp158 and Asn175. Protein Eng. 1994 Jan;7(1):75-82. PMID:8140097
- ↑ [2] University of Maine
- Wang J, Xiang YF, Lim C. The double catalytic triad, Cys25-His159-Asp158 and Cys25-His159-Asn175, in papain catalysis: role of Asp158 and Asn175. Protein Eng. 1994 Jan;7(1):75-82. PMID:8140097
http://www.pdb.org/pdb/explore/explore.do?structureId=2PAD • Show the secondary structures. • Compare the distribution of polar residues to that of nonpolar residues. • Highlight the active site. • If you can find a PDB file of the enzyme that contains a pseudo-substrate (may be inhibitor), highlight it. • Show the contacts or attractions that are present between the pseudo-substrate and the protein, and if the enzyme has multiple subunits, show the contacts between the subunits. • Identify any other ligands that are present in the structure and the types of contacts that are present between them and the protein
http://proteopedia.org/wiki/index.php/Sandbox_55#cite_note-18 Table of contents Pictures References (cross links)
