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5nas

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==Crystal structure of human 14-3-3 zeta in complex with PI4KIIIB peptide==
==Crystal structure of human 14-3-3 zeta in complex with PI4KIIIB peptide==
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<StructureSection load='5nas' size='340' side='right' caption='[[5nas]], [[Resolution|resolution]] 2.08&Aring;' scene=''>
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<StructureSection load='5nas' size='340' side='right'caption='[[5nas]], [[Resolution|resolution]] 2.08&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5nas]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5NAS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5NAS FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5nas]] is a 4 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=5NAS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5NAS FirstGlance]. <br>
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</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=SEP:PHOSPHOSERINE'>SEP</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]] 2.08&#8491;</td></tr>
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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/1-phosphatidylinositol_4-kinase 1-phosphatidylinositol 4-kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.67 2.7.1.67] </span></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=SEP:PHOSPHOSERINE'>SEP</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=5nas FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5nas OCA], [http://pdbe.org/5nas PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5nas RCSB], [http://www.ebi.ac.uk/pdbsum/5nas PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5nas 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=5nas FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5nas OCA], [https://pdbe.org/5nas PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5nas RCSB], [https://www.ebi.ac.uk/pdbsum/5nas PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5nas ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/1433Z_HUMAN 1433Z_HUMAN]] Adapter protein implicated in the regulation of a large spectrum of both general and specialized signaling pathways. Binds to a large number of partners, usually by recognition of a phosphoserine or phosphothreonine motif. Binding generally results in the modulation of the activity of the binding partner.<ref>PMID:9360956</ref> <ref>PMID:14578935</ref> <ref>PMID:15071501</ref> <ref>PMID:15644438</ref> <ref>PMID:16376338</ref> [[http://www.uniprot.org/uniprot/PI4KB_HUMAN PI4KB_HUMAN]] Phosphorylates phosphatidylinositol (PI) in the first committed step in the production of the second messenger inositol-1,4,5,-trisphosphate (PIP). May regulate Golgi disintegration/reorganization during mitosis, possibly via its phosphorylation. Involved in Golgi-to-plasma membrane trafficking (By similarity).<ref>PMID:9405935</ref> <ref>PMID:10559940</ref> <ref>PMID:12749687</ref>
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[https://www.uniprot.org/uniprot/1433Z_HUMAN 1433Z_HUMAN] Adapter protein implicated in the regulation of a large spectrum of both general and specialized signaling pathways. Binds to a large number of partners, usually by recognition of a phosphoserine or phosphothreonine motif. Binding generally results in the modulation of the activity of the binding partner.<ref>PMID:9360956</ref> <ref>PMID:14578935</ref> <ref>PMID:15071501</ref> <ref>PMID:15644438</ref> <ref>PMID:16376338</ref>
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==See Also==
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*[[14-3-3 protein 3D structures|14-3-3 protein 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: 1-phosphatidylinositol 4-kinase]]
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[[Category: Homo sapiens]]
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[[Category: Boura, E]]
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[[Category: Large Structures]]
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[[Category: Eisenreichova, A]]
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[[Category: Boura E]]
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[[Category: Kinase]]
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[[Category: Eisenreichova A]]
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[[Category: Phosphatidylinositol]]
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[[Category: Phosphoserine]]
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[[Category: Regulation]]
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[[Category: Transferase]]
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Current revision

Crystal structure of human 14-3-3 zeta in complex with PI4KIIIB peptide

PDB ID 5nas

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