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2cjx

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<StructureSection load='2cjx' size='340' side='right'caption='[[2cjx]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
<StructureSection load='2cjx' size='340' side='right'caption='[[2cjx]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[2cjx]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CJX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2CJX FirstGlance]. <br>
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<table><tr><td colspan='2'>[[2cjx]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CJX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2CJX FirstGlance]. <br>
</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=0QE:CHLOROMETHANE'>0QE</scene>, <scene name='pdbligand=PHQ:BENZYL+CHLOROCARBONATE'>PHQ</scene></td></tr>
</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=0QE:CHLOROMETHANE'>0QE</scene>, <scene name='pdbligand=PHQ:BENZYL+CHLOROCARBONATE'>PHQ</scene></td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1cp3|1cp3]], [[1gfw|1gfw]], [[1i3o|1i3o]], [[1nme|1nme]], [[1nmq|1nmq]], [[1nms|1nms]], [[1pau|1pau]], [[1qx3|1qx3]], [[1re1|1re1]], [[1rhj|1rhj]], [[1rhk|1rhk]], [[1rhm|1rhm]], [[1rhq|1rhq]], [[1rhr|1rhr]], [[1rhu|1rhu]], [[2c1e|2c1e]], [[2c2k|2c2k]], [[2c2m|2c2m]], [[2c2o|2c2o]], [[2cdr|2cdr]], [[2cjy|2cjy]]</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1cp3|1cp3]], [[1gfw|1gfw]], [[1i3o|1i3o]], [[1nme|1nme]], [[1nmq|1nmq]], [[1nms|1nms]], [[1pau|1pau]], [[1qx3|1qx3]], [[1re1|1re1]], [[1rhj|1rhj]], [[1rhk|1rhk]], [[1rhm|1rhm]], [[1rhq|1rhq]], [[1rhr|1rhr]], [[1rhu|1rhu]], [[2c1e|2c1e]], [[2c2k|2c2k]], [[2c2m|2c2m]], [[2c2o|2c2o]], [[2cdr|2cdr]], [[2cjy|2cjy]]</div></td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Caspase-3 Caspase-3], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.22.56 3.4.22.56] </span></td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Caspase-3 Caspase-3], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.22.56 3.4.22.56] </span></td></tr>
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<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=2cjx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2cjx OCA], [http://pdbe.org/2cjx PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2cjx RCSB], [http://www.ebi.ac.uk/pdbsum/2cjx PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2cjx ProSAT]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2cjx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2cjx OCA], [https://pdbe.org/2cjx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2cjx RCSB], [https://www.ebi.ac.uk/pdbsum/2cjx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2cjx ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/CASP3_HUMAN CASP3_HUMAN]] Involved in the activation cascade of caspases responsible for apoptosis execution. At the onset of apoptosis it proteolytically cleaves poly(ADP-ribose) polymerase (PARP) at a '216-Asp-|-Gly-217' bond. Cleaves and activates sterol regulatory element binding proteins (SREBPs) between the basic helix-loop-helix leucine zipper domain and the membrane attachment domain. Cleaves and activates caspase-6, -7 and -9. Involved in the cleavage of huntingtin. Triggers cell adhesion in sympathetic neurons through RET cleavage.<ref>PMID:7596430</ref> <ref>PMID:21357690</ref>
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[[https://www.uniprot.org/uniprot/CASP3_HUMAN CASP3_HUMAN]] Involved in the activation cascade of caspases responsible for apoptosis execution. At the onset of apoptosis it proteolytically cleaves poly(ADP-ribose) polymerase (PARP) at a '216-Asp-|-Gly-217' bond. Cleaves and activates sterol regulatory element binding proteins (SREBPs) between the basic helix-loop-helix leucine zipper domain and the membrane attachment domain. Cleaves and activates caspase-6, -7 and -9. Involved in the cleavage of huntingtin. Triggers cell adhesion in sympathetic neurons through RET cleavage.<ref>PMID:7596430</ref> <ref>PMID:21357690</ref>
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]

Revision as of 10:01, 12 May 2021

Extended substrate recognition in caspase-3 revealed by high resolution X-ray structure analysis

PDB ID 2cjx

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