1mzk: Difference between revisions

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 ==NMR structure of kinase-interacting FHA domain of kinase associated protein phosphatase, KAPP in Arabidopsis==
-<StructureSection load='1mzk' size='340' side='right' caption='[[1mzk]], [[NMR_Ensembles_of_Models | 30 NMR models]]' scene=''>
+<StructureSection load='1mzk' size='340' side='right'caption='[[1mzk]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1mzk]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Arath Arath]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MZK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1MZK FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1mzk]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MZK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MZK FirstGlance]. <br>
-</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">KAPP ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3702 ARATH])</td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Phosphoprotein_phosphatase Phosphoprotein phosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.16 3.1.3.16] </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=1mzk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mzk OCA], [https://pdbe.org/1mzk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1mzk RCSB], [https://www.ebi.ac.uk/pdbsum/1mzk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1mzk ProSAT]</span></td></tr>
-<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=1mzk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mzk OCA], [http://pdbe.org/1mzk PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1mzk RCSB], [http://www.ebi.ac.uk/pdbsum/1mzk PDBsum]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/P2C70_ARATH P2C70_ARATH]] Dephosphorylates the Ser/Thr receptor-like kinase RLK5. May function as a signaling component in a pathway involving RLK5 (PubMed:15592873). Binds and dephosphorylates CLAVATA1 (CLV1). Functions as a negative regulator of the CLV1 signaling in plant development (PubMed:9294234, PubMed:9701578). Dephosphorylates SERK1 receptor kinase on threonine residues in the A-loop. Dephosphorylation of SERK1 controls SERK1 internalization (PubMed:12101128). Component of a signaling pathway which mediates adaptation to NaCl stress. Is not a component of the SALT OVERLY SENSITIVE (SOS) pathway (PubMed:18162596).<ref>PMID:12101128</ref> <ref>PMID:15592873</ref> <ref>PMID:18162596</ref> <ref>PMID:9294234</ref> <ref>PMID:9701578</ref>
+[https://www.uniprot.org/uniprot/P2C70_ARATH P2C70_ARATH] Dephosphorylates the Ser/Thr receptor-like kinase RLK5. May function as a signaling component in a pathway involving RLK5 (PubMed:15592873). Binds and dephosphorylates CLAVATA1 (CLV1). Functions as a negative regulator of the CLV1 signaling in plant development (PubMed:9294234, PubMed:9701578). Dephosphorylates SERK1 receptor kinase on threonine residues in the A-loop. Dephosphorylation of SERK1 controls SERK1 internalization (PubMed:12101128). Component of a signaling pathway which mediates adaptation to NaCl stress. Is not a component of the SALT OVERLY SENSITIVE (SOS) pathway (PubMed:18162596).<ref>PMID:12101128</ref> <ref>PMID:15592873</ref> <ref>PMID:18162596</ref> <ref>PMID:9294234</ref> <ref>PMID:9701578</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
 Check<jmol>
    <jmolCheckbox>
-     <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/mz/1mzk_consurf.spt"</scriptWhenChecked>
+     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/mz/1mzk_consurf.spt"</scriptWhenChecked>
      <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
      <text>to colour the structure by Evolutionary Conservation</text>
@@ Line 32: / Line 32: @@
 __TOC__
 </StructureSection>
-[[Category: Arath]]
+[[Category: Arabidopsis thaliana]]
-[[Category: Phosphoprotein phosphatase]]
+[[Category: Large Structures]]
-[[Category: Ding, Z]]
+[[Category: Ding Z]]
-[[Category: Doren, S R.Van]]
+[[Category: Lee G]]
-[[Category: Lee, G]]
+[[Category: Van Doren SR]]
-[[Category: Walker, J C]]
+[[Category: Walker JC]]
-[[Category: Beta sandwich]]
-[[Category: Hydrolase]]