1oet: Difference between revisions

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<StructureSection load='1oet' size='340' side='right'caption='[[1oet]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
<StructureSection load='1oet' size='340' side='right'caption='[[1oet]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1oet]] 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=1OET OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1OET FirstGlance]. <br>
<table><tr><td colspan='2'>[[1oet]] 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=1OET OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1OET FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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]] 2.3&#8491;</td></tr>
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CSO:S-HYDROXYCYSTEINE'>CSO</scene></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CSO:S-HYDROXYCYSTEINE'>CSO</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1a5y|1a5y]], [[1aax|1aax]], [[1bzc|1bzc]], [[1bzh|1bzh]], [[1bzj|1bzj]], [[1c83|1c83]], [[1c84|1c84]], [[1c85|1c85]], [[1c86|1c86]], [[1c87|1c87]], [[1c88|1c88]], [[1ecv|1ecv]], [[1een|1een]], [[1eeo|1eeo]], [[1g1f|1g1f]], [[1g1g|1g1g]], [[1g1h|1g1h]], [[1g7f|1g7f]], [[1g7g|1g7g]], [[1gfy|1gfy]], [[1i57|1i57]], [[1jf7|1jf7]], [[1kak|1kak]], [[1kav|1kav]], [[1l8g|1l8g]], [[1lqf|1lqf]], [[1n6w|1n6w]], [[1oem|1oem]], [[1oeo|1oeo]], [[1oes|1oes]], [[1oeu|1oeu]], [[1oev|1oev]], [[1ptt|1ptt]], [[1ptu|1ptu]], [[1ptv|1ptv]], [[1pty|1pty]], [[2hnp|2hnp]], [[2hnq|2hnq]]</div></td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Protein-tyrosine-phosphatase Protein-tyrosine-phosphatase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.48 3.1.3.48] </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=1oet FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1oet OCA], [https://pdbe.org/1oet PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1oet RCSB], [https://www.ebi.ac.uk/pdbsum/1oet PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1oet 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=1oet FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1oet OCA], [https://pdbe.org/1oet PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1oet RCSB], [https://www.ebi.ac.uk/pdbsum/1oet PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1oet ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/PTN1_HUMAN PTN1_HUMAN]] Tyrosine-protein phosphatase which acts as a regulator of endoplasmic reticulum unfolded protein response. Mediates dephosphorylation of EIF2AK3/PERK; inactivating the protein kinase activity of EIF2AK3/PERK. May play an important role in CKII- and p60c-src-induced signal transduction cascades. May regulate the EFNA5-EPHA3 signaling pathway which modulates cell reorganization and cell-cell repulsion.<ref>PMID:21135139</ref> <ref>PMID:22169477</ref>
[https://www.uniprot.org/uniprot/PTN1_HUMAN PTN1_HUMAN] Tyrosine-protein phosphatase which acts as a regulator of endoplasmic reticulum unfolded protein response. Mediates dephosphorylation of EIF2AK3/PERK; inactivating the protein kinase activity of EIF2AK3/PERK. May play an important role in CKII- and p60c-src-induced signal transduction cascades. May regulate the EFNA5-EPHA3 signaling pathway which modulates cell reorganization and cell-cell repulsion.<ref>PMID:21135139</ref> <ref>PMID:22169477</ref>  
== 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: Protein-tyrosine-phosphatase]]
[[Category: Carr R]]
[[Category: Carr, R]]
[[Category: Congreve M]]
[[Category: Congreve, M]]
[[Category: Jhoti H]]
[[Category: Jhoti, H]]
[[Category: Tisi D]]
[[Category: Montfort, R L.M van]]
[[Category: Van Montfort RLM]]
[[Category: Tisi, D]]
[[Category: Hydrolase]]
[[Category: Oxidative regulation]]
[[Category: Phosphorylation]]
[[Category: Protein tyrosine phosphatase]]