4h57: Difference between revisions
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==Thermolysin inhibition== | ==Thermolysin inhibition== | ||
<StructureSection load='4h57' size='340' side='right' caption='[[4h57]], [[Resolution|resolution]] 1.56Å' scene=''> | <StructureSection load='4h57' size='340' side='right' caption='[[4h57]], [[Resolution|resolution]] 1.56Å' scene=''> | ||
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3fvp|3fvp]], [[3fv4|3fv4]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3fvp|3fvp]], [[3fv4|3fv4]]</td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Thermolysin Thermolysin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.24.27 3.4.24.27] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Thermolysin Thermolysin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.24.27 3.4.24.27] </span></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4h57 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4h57 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4h57 RCSB], [http://www.ebi.ac.uk/pdbsum/4h57 PDBsum]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4h57 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4h57 OCA], [http://pdbe.org/4h57 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4h57 RCSB], [http://www.ebi.ac.uk/pdbsum/4h57 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4h57 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 4h57" style="background-color:#fffaf0;"></div> | |||
==See Also== | ==See Also== | ||
Revision as of 18:42, 4 August 2016
Thermolysin inhibitionThermolysin inhibition
Structural highlights
Function[THER_BACTH] Extracellular zinc metalloprotease. Publication Abstract from PubMedThe hydrophobic effect is associated with the successive replacement of water molecules in the binding site of a protein by hydrophobic groups of the ligand. Although the hydrophobic effect is assumed to be entropy-driven, large changes in enthalpy and entropy are observed with the model system thermolysin. Structural changes in the binding features of the water molecules ultimately determine the thermodynamics of the hydrophobic effect. Dissecting the hydrophobic effect on the molecular level: the role of water, enthalpy, and entropy in ligand binding to thermolysin.,Biela A, Nasief NN, Betz M, Heine A, Hangauer D, Klebe G Angew Chem Int Ed Engl. 2013 Feb 4;52(6):1822-8. doi: 10.1002/anie.201208561., Epub 2013 Jan 2. PMID:23283700[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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