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1atl
From Proteopedia
(Difference between revisions)
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<StructureSection load='1atl' size='340' side='right'caption='[[1atl]], [[Resolution|resolution]] 1.80Å' scene=''> | <StructureSection load='1atl' size='340' side='right'caption='[[1atl]], [[Resolution|resolution]] 1.80Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[1atl]] is a 2 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[1atl]] 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=1ATL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ATL FirstGlance]. <br> |
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=0QI:O-METHYL-N-[(2S)-4-METHYL-2-(SULFANYLMETHYL)PENTANOYL]-L-TYROSINE'>0QI</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=0QI:O-METHYL-N-[(2S)-4-METHYL-2-(SULFANYLMETHYL)PENTANOYL]-L-TYROSINE'>0QI</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | ||
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | <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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1atl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1atl OCA], [https://pdbe.org/1atl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1atl RCSB], [https://www.ebi.ac.uk/pdbsum/1atl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1atl 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> |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Revision as of 10:49, 6 April 2022
Structural interaction of natural and synthetic inhibitors with the VENOM METALLOPROTEINASE, ATROLYSIN C (FORM-D)
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