4h57
From Proteopedia
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| - | [[ | + | ==Thermolysin inhibition== |
| + | <StructureSection load='4h57' size='340' side='right' caption='[[4h57]], [[Resolution|resolution]] 1.56Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[4h57]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Bacillus_thermoproteolyticus Bacillus thermoproteolyticus]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=3fwd 3fwd]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4H57 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4H57 FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=0PJ:N-[(S)-({[(BENZYLOXY)CARBONYL]AMINO}METHYL)(HYDROXY)PHOSPHORYL]-L-LEUCYL-L-LEUCINE'>0PJ</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=DMS:DIMETHYL+SULFOXIDE'>DMS</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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='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> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The 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<ref>PMID:23283700</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
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==See Also== | ==See Also== | ||
*[[Thermolysin|Thermolysin]] | *[[Thermolysin|Thermolysin]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Bacillus thermoproteolyticus]] | [[Category: Bacillus thermoproteolyticus]] | ||
[[Category: Thermolysin]] | [[Category: Thermolysin]] | ||
| - | [[Category: Biela, A | + | [[Category: Biela, A]] |
| - | [[Category: Englert, L | + | [[Category: Englert, L]] |
| - | [[Category: Heine, A | + | [[Category: Heine, A]] |
| - | [[Category: Klebe, G | + | [[Category: Klebe, G]] |
[[Category: Hydrolase-hydrolase inhibitor complex]] | [[Category: Hydrolase-hydrolase inhibitor complex]] | ||
[[Category: Metal-binding]] | [[Category: Metal-binding]] | ||
Revision as of 09:12, 10 December 2014
Thermolysin inhibition
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