3c9q: Difference between revisions

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-[[Image:3c9q.jpg|left|200px]]
- {{Structure
+==Crystal structure of the uncharacterized human protein C8orf32 with bound peptide==
-|PDB= 3c9q |SIZE=350|CAPTION= <scene name='initialview01'>3c9q</scene>, resolution 1.50&Aring;
+<StructureSection load='3c9q' size='340' side='right'caption='[[3c9q]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
-|SITE= <scene name='pdbsite=AC1:So4+Binding+Site+For+Residue+A+206'>AC1</scene>, <scene name='pdbsite=AC2:So4+Binding+Site+For+Residue+A+207'>AC2</scene>, <scene name='pdbsite=AC3:So4+Binding+Site+For+Residue+A+208'>AC3</scene>, <scene name='pdbsite=AC4:So4+Binding+Site+For+Residue+A+209'>AC4</scene>, <scene name='pdbsite=AC5:So4+Binding+Site+For+Residue+A+210'>AC5</scene>, <scene name='pdbsite=AC6:Co3+Binding+Site+For+Residue+A+211'>AC6</scene>, <scene name='pdbsite=AC7:Edo+Binding+Site+For+Residue+A+212'>AC7</scene>, <scene name='pdbsite=AC8:Edo+Binding+Site+For+Residue+A+213'>AC8</scene>, <scene name='pdbsite=AC9:Edo+Binding+Site+For+Residue+A+214'>AC9</scene>, <scene name='pdbsite=BC1:Edo+Binding+Site+For+Residue+A+215'>BC1</scene> and <scene name='pdbsite=BC2:Edo+Binding+Site+For+Residue+A+216'>BC2</scene>
+== Structural highlights ==
-|LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=CO3:CARBONATE+ION'>CO3</scene> and <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>
+<table><tr><td colspan='2'>[[3c9q]] 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=3C9Q OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3C9Q FirstGlance]. <br>
-|ACTIVITY=
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.5&#8491;</td></tr>
-|GENE= C8orf32 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CO3:CARBONATE+ION'>CO3</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=3c9q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3c9q OCA], [https://pdbe.org/3c9q PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3c9q RCSB], [https://www.ebi.ac.uk/pdbsum/3c9q PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3c9q ProSAT], [https://www.topsan.org/Proteins/CESG/3c9q TOPSAN]</span></td></tr>
+</table>
-'''Crystal structure of the uncharacterized human protein C8orf32 with bound peptide'''
+== Function ==
+[https://www.uniprot.org/uniprot/NTAQ1_HUMAN NTAQ1_HUMAN] Mediates the side-chain deamidation of N-terminal glutamine residues to glutamate, an important step in N-end rule pathway of protein degradation. Conversion of the resulting N-terminal glutamine to glutamate renders the protein susceptible to arginylation, polyubiquitination and degradation as specified by the N-end rule. Does not act on substrates with internal or C-terminal glutamine and does not act on non-glutamine residues in any position. Does not deaminate acetylated N-terminal glutamine. With the exception of proline, all tested second-position residues on substrate peptides do not greatly influence the activity. In contrast, a proline at position 2, virtually abolishes deamidation of N-terminal glutamine (By similarity).
+== Evolutionary Conservation ==
-==About this Structure==
+[[Image:Consurf_key_small.gif|200px|right]]
-C9Q is a [[Protein complex]] structure of sequences 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=3C9Q OCA].
+Check<jmol>
+  <jmolCheckbox>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/c9/3c9q_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
+    <text>to colour the structure by Evolutionary Conservation</text>
+  </jmolCheckbox>
+</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=3c9q ConSurf].
+<div style="clear:both"></div>
+__TOC__
+</StructureSection>
 [[Category: Homo sapiens]]
-[[Category: Protein complex]]
+[[Category: Large Structures]]
-[[Category: Bingman, C A.]]
+[[Category: Bingman CA]]
-[[Category: Bitto, E.]]
+[[Category: Bitto E]]
-[[Category: CESG, Center for Eukaryotic Structural Genomics.]]
+[[Category: McCoy JG]]
-[[Category: Jr., G N.Phillips.]]
+[[Category: Phillips Jr GN]]
-[[Category: McCoy, J G.]]
+[[Category: Wesenberg GE]]
-[[Category: Wesenberg, G E.]]
-[[Category: CO3]]
-[[Category: EDO]]
-[[Category: SO4]]
-[[Category: candidate gene important in the pathogenesis of t-cell prolymphocytic leukemia]]
-[[Category: center for eukaryotic structural genomic]]
-[[Category: cesg]]
-[[Category: gene associated with cre-pathway activation]]
-[[Category: medically relevant]]
-[[Category: protein structure initiative]]
-[[Category: psi-2]]
-[[Category: putative involvement in human inherited ataxias and disorders of purkinje cell degeneration]]
-[[Category: structural genomic]]
-[[Category: unknown function]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 19:03:05 2008''