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5jg8

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'''Unreleased structure'''
 
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The entry 5jg8 is ON HOLD until Paper Publication
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==Crystal structure of human acid sphingomyelinase==
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<StructureSection load='5jg8' size='340' side='right' caption='[[5jg8]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
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Authors:
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== Structural highlights ==
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<table><tr><td colspan='2'>[[5jg8]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5JG8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5JG8 FirstGlance]. <br>
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Description:
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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[[Category: Unreleased Structures]]
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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/Sphingomyelin_phosphodiesterase Sphingomyelin phosphodiesterase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.4.12 3.1.4.12] </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=5jg8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5jg8 OCA], [http://pdbe.org/5jg8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5jg8 RCSB], [http://www.ebi.ac.uk/pdbsum/5jg8 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5jg8 ProSAT]</span></td></tr>
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</table>
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== Disease ==
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[[http://www.uniprot.org/uniprot/ASM_HUMAN ASM_HUMAN]] Niemann-Pick disease type A;Niemann-Pick disease type B. The disease is caused by mutations affecting the gene represented in this entry. The disease is caused by mutations affecting the gene represented in this entry.
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== Function ==
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[[http://www.uniprot.org/uniprot/ASM_HUMAN ASM_HUMAN]] Converts sphingomyelin to ceramide (PubMed:1840600, PubMed:18815062). Also has phospholipase C activities toward 1,2-diacylglycerolphosphocholine and 1,2-diacylglycerolphosphoglycerol.<ref>PMID:1840600</ref> <ref>PMID:18815062</ref> Isoform 2 lacks residues that bind the cofactor Zn(2+) and has no enzyme activity.<ref>PMID:1840600</ref> Isoform 3 lacks residues that bind the cofactor Zn(2+) and has no enzyme activity.<ref>PMID:1840600</ref>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Sphingomyelin phosphodiesterase]]
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[[Category: Prive, G G]]
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[[Category: Xiong, Z J]]
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[[Category: Hydrolase]]
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[[Category: Lysosomal hydrolase]]
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[[Category: Neimann-pick disease]]
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[[Category: Saposin]]
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[[Category: Sphingolipid]]

Revision as of 03:07, 13 July 2016

Crystal structure of human acid sphingomyelinase

5jg8, resolution 2.80Å

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