2xph

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[[Image:2xph.png|left|200px]]
 
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==Crystal structure of human SENP1 with the bound cobalt==
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The line below this paragraph, containing "STRUCTURE_2xph", creates the "Structure Box" on the page.
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<StructureSection load='2xph' size='340' side='right'caption='[[2xph]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[2xph]] is a 2 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=2XPH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2XPH FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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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]] 2.4&#8491;</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=CO:COBALT+(II)+ION'>CO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>
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{{STRUCTURE_2xph| PDB=2xph | SCENE= }}
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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=2xph FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xph OCA], [https://pdbe.org/2xph PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2xph RCSB], [https://www.ebi.ac.uk/pdbsum/2xph PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2xph ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/SENP1_HUMAN SENP1_HUMAN] Protease that catalyzes two essential functions in the SUMO pathway: processing of full-length SUMO1, SUMO2 and SUMO3 to their mature forms and deconjugation of SUMO1, SUMO2 and SUMO3 from targeted proteins. Deconjugates SUMO1 from HIPK2. Deconjugates SUMO1 from HDAC1, which decreases its transcriptional repression activity.<ref>PMID:10652325</ref> <ref>PMID:15199155</ref> <ref>PMID:16253240</ref> <ref>PMID:16553580</ref>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/xp/2xph_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2xph ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Metal ions often stabilize intermolecular contacts between macromolecules, thereby promoting crystallization. When interpreting a medium-resolution electron-density map of the catalytic domain of human sentrin-specific protease 1 (SENP1), a strong feature indicative of an ordered divalent cation was noted. This was assigned as Co(2+), an essential component of the crystallization mixture. The ion displays tetrahedral coordination by Glu430 and His640 from one molecule and the corresponding residues from a symmetry-related molecule. Analysis of the data derived from a previous structure of SENP1 suggested that Co(2+) had been overlooked and re-refinement supported this conclusion. High-throughput automated re-refinement protocols also failed to mark the Co(2+) position, supporting the requirement for the incorporation of as much information as possible to enhance the value of such protocols.
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===Crystal structure of human SENP1 with the bound cobalt===
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The role of Co(2)+ in the crystallization of human SENP1 and comments on the limitations of automated refinement protocols.,Rimsa V, Eadsforth T, Hunter WN Acta Crystallogr Sect F Struct Biol Cryst Commun. 2011 Apr 1;67(Pt 4):442-5. Epub, 2011 Mar 24. PMID:21505236<ref>PMID:21505236</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 2xph" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_21505236}}, adds the Publication Abstract to the page
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*[[Sentrin-specific protease|Sentrin-specific protease]]
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(as it appears on PubMed at http://www.pubmed.gov), where 21505236 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_21505236}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[2xph]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2XPH OCA].
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==Reference==
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<ref group="xtra">PMID:021505236</ref><references group="xtra"/>
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Eadsforth, T.]]
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[[Category: Large Structures]]
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[[Category: Hay, R T.]]
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[[Category: Eadsforth T]]
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[[Category: Hunter, W N.]]
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[[Category: Hay RT]]
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[[Category: Rimsa, V.]]
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[[Category: Hunter WN]]
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[[Category: Cysteine protease]]
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[[Category: Rimsa V]]
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[[Category: Hydrolase]]
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[[Category: Thiol protease]]
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Current revision

Crystal structure of human SENP1 with the bound cobalt

PDB ID 2xph

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OCA

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