5ibc: Difference between revisions

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 ==Caspase 3 V266I==
-<StructureSection load='5ibc' size='340' side='right' caption='[[5ibc]], [[Resolution|resolution]] 1.66&Aring;' scene=''>
+<StructureSection load='5ibc' size='340' side='right'caption='[[5ibc]], [[Resolution|resolution]] 1.66&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[5ibc]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5IBC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5IBC FirstGlance]. <br>
+<table><tr><td colspan='2'>[[5ibc]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Unidentified Unidentified]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5IBC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5IBC FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</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]] 1.66&#8491;</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=ACE:ACETYL+GROUP'>ACE</scene></td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=0QE:CHLOROMETHANE'>0QE</scene>, <scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>
-<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>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5ibc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ibc OCA], [https://pdbe.org/5ibc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ibc RCSB], [https://www.ebi.ac.uk/pdbsum/5ibc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ibc ProSAT]</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=5ibc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ibc OCA], [http://pdbe.org/5ibc PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ibc RCSB], [http://www.ebi.ac.uk/pdbsum/5ibc PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5ibc ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[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>
+[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>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 20: / Line 19: @@
 </div>
 <div class="pdbe-citations 5ibc" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Caspase 3D structures|Caspase 3D structures]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Caspase-3]]
+[[Category: Homo sapiens]]
-[[Category: Clark, A C]]
+[[Category: Large Structures]]
-[[Category: Maciag, J J]]
+[[Category: Unidentified]]
-[[Category: Mackenzie, S H]]
+[[Category: Clark AC]]
-[[Category: Schipper, J L]]
+[[Category: Maciag JJ]]
-[[Category: Swartz, P D]]
+[[Category: Mackenzie SH]]
-[[Category: Tucker, M B]]
+[[Category: Schipper JL]]
-[[Category: Allostery]]
+[[Category: Swartz PD]]
-[[Category: Conformational selection]]
+[[Category: Tucker MB]]
-[[Category: Hydrolase-hydrolase inhibitor complex]]
-[[Category: Native ensemble]]
-[[Category: Protein dynamic]]
-[[Category: Protein solvation]]
-[[Category: Protein structure]]
-[[Category: Saturation mutagenesis]]