3f01: Difference between revisions

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<StructureSection load='3f01' size='340' side='right'caption='[[3f01]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
<StructureSection load='3f01' size='340' side='right'caption='[[3f01]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3f01]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3F01 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3F01 FirstGlance]. <br>
<table><tr><td colspan='2'>[[3f01]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3F01 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3F01 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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]] 1.7&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3f00|3f00]], [[3f04|3f04]], [[3f05|3f05]]</div></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SYT1, SVP65, SYT ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=3f01 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3f01 OCA], [https://pdbe.org/3f01 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3f01 RCSB], [https://www.ebi.ac.uk/pdbsum/3f01 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3f01 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=3f01 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3f01 OCA], [https://pdbe.org/3f01 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3f01 RCSB], [https://www.ebi.ac.uk/pdbsum/3f01 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3f01 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/SYT1_HUMAN SYT1_HUMAN]] May have a regulatory role in the membrane interactions during trafficking of synaptic vesicles at the active zone of the synapse. It binds acidic phospholipids with a specificity that requires the presence of both an acidic head group and a diacyl backbone. A Ca(2+)-dependent interaction between synaptotagmin and putative receptors for activated protein kinase C has also been reported. It can bind to at least three additional proteins in a Ca(2+)-independent manner; these are neurexins, syntaxin and AP2.  
[https://www.uniprot.org/uniprot/SYT1_HUMAN SYT1_HUMAN] May have a regulatory role in the membrane interactions during trafficking of synaptic vesicles at the active zone of the synapse. It binds acidic phospholipids with a specificity that requires the presence of both an acidic head group and a diacyl backbone. A Ca(2+)-dependent interaction between synaptotagmin and putative receptors for activated protein kinase C has also been reported. It can bind to at least three additional proteins in a Ca(2+)-independent manner; these are neurexins, syntaxin and AP2.
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Human]]
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Dakshinamurthy, R]]
[[Category: Dakshinamurthy R]]
[[Category: Guo, F]]
[[Category: Guo F]]
[[Category: Sakon, J]]
[[Category: Sakon J]]
[[Category: Thallapuranam, S K.K]]
[[Category: Thallapuranam SKK]]
[[Category: C2a]]
[[Category: Calcium]]
[[Category: Cell junction]]
[[Category: Copper]]
[[Category: Cytoplasmic vesicle]]
[[Category: Glycoprotein]]
[[Category: Lipoprotein]]
[[Category: Membrane]]
[[Category: Metal binding protein]]
[[Category: Metal-binding]]
[[Category: Palmitate]]
[[Category: Phosphoprotein]]
[[Category: Synapse]]
[[Category: Synaptotagmin i]]
[[Category: Transmembrane]]

Latest revision as of 06:39, 6 September 2023

Crystal Structure of Synaptotagmin I C2A domain with Cu(II)

3f01, resolution 1.70Å

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