1dth: Difference between revisions

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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1dth]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Crotalus_atrox Crotalus atrox]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DTH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DTH FirstGlance]. <br>
<table><tr><td colspan='2'>[[1dth]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Crotalus_atrox Crotalus atrox]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DTH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DTH FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BAT:4-(N-HYDROXYAMINO)-2R-ISOBUTYL-2S-(2-THIENYLTHIOMETHYL)SUCCINYL-L-PHENYLALANINE-N-METHYLAMIDE'>BAT</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2&#8491;</td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Atrolysin_C Atrolysin C], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.24.42 3.4.24.42] </span></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BAT:4-(N-HYDROXYAMINO)-2R-ISOBUTYL-2S-(2-THIENYLTHIOMETHYL)SUCCINYL-L-PHENYLALANINE-N-METHYLAMIDE'>BAT</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1dth FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dth OCA], [https://pdbe.org/1dth PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1dth RCSB], [https://www.ebi.ac.uk/pdbsum/1dth PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1dth ProSAT]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1dth FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dth OCA], [https://pdbe.org/1dth PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1dth RCSB], [https://www.ebi.ac.uk/pdbsum/1dth PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1dth ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/VM1AD_CROAT VM1AD_CROAT]] Snake venom zinc metalloproteinase that causes hemorrhage by provoking the degradation of the sub-endothelial matrix proteins (fibronectin, laminin, type IV collagen, nidogen, and gelatins).<ref>PMID:2817904</ref>
[https://www.uniprot.org/uniprot/VM1AD_CROAT VM1AD_CROAT] Snake venom zinc metalloproteinase that causes hemorrhage by provoking the degradation of the sub-endothelial matrix proteins (fibronectin, laminin, type IV collagen, nidogen, and gelatins).<ref>PMID:2817904</ref>  
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1dth ConSurf].
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1dth ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Matrix metalloproteinase enzymes have been implicated in degenerative processes like tumor cell invasion, metastasis, and arthritis. Specific metalloproteinase inhibitors have been used to block tumor cell proliferation. We have examined the interaction of batimastat (BB-94) with a metalloproteinase [atrolysin C (Ht-d), EC 3.4.24.42] active site at 2.0-angstroms resolution (R = 16.8%). The title structure exhibits an unexpected binding geometry, with the thiophene ring deeply inserted into the primary specificity site. This unprecedented binding geometry dramatizes the significance of the cavernous primary specificity site, pointing the way for the design of a new generation of potential antitumor drugs.
Batimastat, a potent matrix mealloproteinase inhibitor, exhibits an unexpected mode of binding.,Botos I, Scapozza L, Zhang D, Liotta LA, Meyer EF Proc Natl Acad Sci U S A. 1996 Apr 2;93(7):2749-54. PMID:8610113<ref>PMID:8610113</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1dth" style="background-color:#fffaf0;"></div>
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Atrolysin C]]
[[Category: Crotalus atrox]]
[[Category: Crotalus atrox]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Botos, I]]
[[Category: Botos I]]
[[Category: Liotta, L A]]
[[Category: Liotta LA]]
[[Category: Meyer, E F]]
[[Category: Meyer EF]]
[[Category: Scapozza, L]]
[[Category: Scapozza L]]
[[Category: Zhang, D]]
[[Category: Zhang D]]
[[Category: Hydrolase]]
[[Category: Metalloprotease]]
[[Category: Venom]]
[[Category: Zinc]]

Revision as of 09:53, 20 March 2024

METALLOPROTEASE

1dth, resolution 2.00Å

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