5uvg

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==Crystal structure of the human neutral sphingomyelinase 2 (nSMase2) catalytic domain with insertion deleted and calcium bound==
==Crystal structure of the human neutral sphingomyelinase 2 (nSMase2) catalytic domain with insertion deleted and calcium bound==
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<StructureSection load='5uvg' size='340' side='right' caption='[[5uvg]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
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<StructureSection load='5uvg' size='340' side='right'caption='[[5uvg]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5uvg]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5UVG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5UVG FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5uvg]] 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=5UVG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5UVG FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.849&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SMPD3 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></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=5uvg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5uvg OCA], [http://pdbe.org/5uvg PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5uvg RCSB], [http://www.ebi.ac.uk/pdbsum/5uvg PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5uvg 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=5uvg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5uvg OCA], [https://pdbe.org/5uvg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5uvg RCSB], [https://www.ebi.ac.uk/pdbsum/5uvg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5uvg ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/NSMA2_HUMAN NSMA2_HUMAN]] Catalyzes the hydrolysis of sphingomyelin to form ceramide and phosphocholine. Ceramide mediates numerous cellular functions, such as apoptosis and growth arrest, and is capable of regulating these 2 cellular events independently. Also hydrolyzes sphingosylphosphocholine. Regulates the cell cycle by acting as a growth suppressor in confluent cells. Probably acts as a regulator of postnatal development and participates in bone and dentin mineralization.<ref>PMID:10823942</ref> <ref>PMID:14741383</ref> <ref>PMID:15051724</ref>
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[https://www.uniprot.org/uniprot/NSMA2_HUMAN NSMA2_HUMAN] Catalyzes the hydrolysis of sphingomyelin to form ceramide and phosphocholine. Ceramide mediates numerous cellular functions, such as apoptosis and growth arrest, and is capable of regulating these 2 cellular events independently. Also hydrolyzes sphingosylphosphocholine. Regulates the cell cycle by acting as a growth suppressor in confluent cells. Probably acts as a regulator of postnatal development and participates in bone and dentin mineralization.<ref>PMID:10823942</ref> <ref>PMID:14741383</ref> <ref>PMID:15051724</ref>
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==See Also==
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*[[Sphingomyelinase|Sphingomyelinase]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Human]]
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[[Category: Homo sapiens]]
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[[Category: Airola, M V]]
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[[Category: Large Structures]]
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[[Category: Garcia-Diaz, M]]
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[[Category: Airola MV]]
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[[Category: Guja, K E]]
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[[Category: Garcia-Diaz M]]
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[[Category: Hannun, Y A]]
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[[Category: Guja KE]]
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[[Category: Hydrolase]]
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[[Category: Hannun YA]]
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[[Category: Sphingomyelinase]]
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Current revision

Crystal structure of the human neutral sphingomyelinase 2 (nSMase2) catalytic domain with insertion deleted and calcium bound

PDB ID 5uvg

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