7bj1

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<StructureSection load='7bj1' size='340' side='right'caption='[[7bj1]], [[Resolution|resolution]] 1.61&Aring;' scene=''>
<StructureSection load='7bj1' size='340' side='right'caption='[[7bj1]], [[Resolution|resolution]] 1.61&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[7bj1]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=6z2r 6z2r]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7BJ1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7BJ1 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[7bj1]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=6z2r 6z2r]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7BJ1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7BJ1 FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=QKT:Diperodon+(S-enantiomer)'>QKT</scene>, <scene name='pdbligand=SAM:S-ADENOSYLMETHIONINE'>SAM</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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]] 1.61&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SMYD3, ZMYND1, ZNFN3A1 ([https://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=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=QKT:Diperodon+(S-enantiomer)'>QKT</scene>, <scene name='pdbligand=SAM:S-ADENOSYLMETHIONINE'>SAM</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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/[Histone_H3]-lysine(4)_N-trimethyltransferase [Histone H3]-lysine(4) N-trimethyltransferase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.354 2.1.1.354] </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=7bj1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7bj1 OCA], [https://pdbe.org/7bj1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7bj1 RCSB], [https://www.ebi.ac.uk/pdbsum/7bj1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7bj1 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=7bj1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7bj1 OCA], [https://pdbe.org/7bj1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7bj1 RCSB], [https://www.ebi.ac.uk/pdbsum/7bj1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7bj1 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/SMYD3_HUMAN SMYD3_HUMAN]] Histone methyltransferase. Specifically methylates 'Lys-4' and 'Lys-5' of histone H3, inducing di- and tri-methylation, but not monomethylation. Plays an important role in transcriptional activation as a member of an RNA polymerase complex. Binds DNA containing 5'-CCCTCC-3' or 5'-GAGGGG-3' sequences.<ref>PMID:15235609</ref> <ref>PMID:22419068</ref>
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[https://www.uniprot.org/uniprot/SMYD3_HUMAN SMYD3_HUMAN] Histone methyltransferase. Specifically methylates 'Lys-4' and 'Lys-5' of histone H3, inducing di- and tri-methylation, but not monomethylation. Plays an important role in transcriptional activation as a member of an RNA polymerase complex. Binds DNA containing 5'-CCCTCC-3' or 5'-GAGGGG-3' sequences.<ref>PMID:15235609</ref> <ref>PMID:22419068</ref>
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Human]]
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[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Cederfelt, D]]
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[[Category: Cederfelt D]]
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[[Category: Danielson, U H]]
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[[Category: Danielson UH]]
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[[Category: Dobritzsch, D]]
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[[Category: Dobritzsch D]]
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[[Category: Talibov, V O]]
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[[Category: Talibov VO]]
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[[Category: Complex]]
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[[Category: Inhibitor]]
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[[Category: Methyltransferase]]
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[[Category: Oncoprotein]]
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Current revision

Crystal structure of SMYD3 with diperodon S enantiomer bound to allosteric site

PDB ID 7bj1

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