2yxe

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==Crystal structure of L-isoaspartyl protein carboxyl methyltranferase==
==Crystal structure of L-isoaspartyl protein carboxyl methyltranferase==
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<StructureSection load='2yxe' size='340' side='right' caption='[[2yxe]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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<StructureSection load='2yxe' size='340' side='right'caption='[[2yxe]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[2yxe]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Methanocaldococcus_jannaschii Methanocaldococcus jannaschii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2YXE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2YXE FirstGlance]. <br>
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<table><tr><td colspan='2'>[[2yxe]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Methanocaldococcus_jannaschii_DSM_2661 Methanocaldococcus jannaschii DSM 2661]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2YXE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2YXE FirstGlance]. <br>
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</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene><br>
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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&#8491;</td></tr>
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<tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">pcm ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2190 Methanocaldococcus jannaschii])</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=ACT:ACETATE+ION'>ACT</scene></td></tr>
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<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Protein-L-isoaspartate(D-aspartate)_O-methyltransferase Protein-L-isoaspartate(D-aspartate) O-methyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.77 2.1.1.77] </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=2yxe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2yxe OCA], [https://pdbe.org/2yxe PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2yxe RCSB], [https://www.ebi.ac.uk/pdbsum/2yxe PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2yxe ProSAT], [https://www.topsan.org/Proteins/RSGI/2yxe TOPSAN]</span></td></tr>
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<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2yxe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2yxe OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2yxe RCSB], [http://www.ebi.ac.uk/pdbsum/2yxe PDBsum], [http://www.topsan.org/Proteins/RSGI/2yxe TOPSAN]</span></td></tr>
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</table>
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<table>
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== Function ==
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[https://www.uniprot.org/uniprot/PIMT_METJA PIMT_METJA] Catalyzes the methyl esterification of L-isoaspartyl residues in peptides and proteins that result from spontaneous decomposition of normal L-aspartyl and L-asparaginyl residues. It plays a role in the repair and/or degradation of damaged proteins (By similarity).
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
Check<jmol>
<jmolCheckbox>
<jmolCheckbox>
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<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/yx/2yxe_consurf.spt"</scriptWhenChecked>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/yx/2yxe_consurf.spt"</scriptWhenChecked>
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
<text>to colour the structure by Evolutionary Conservation</text>
<text>to colour the structure by Evolutionary Conservation</text>
</jmolCheckbox>
</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/chain_selection.php?pdb_ID=2ata ConSurf].
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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=2yxe ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Methanocaldococcus jannaschii]]
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[[Category: Large Structures]]
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[[Category: Bessho, Y.]]
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[[Category: Methanocaldococcus jannaschii DSM 2661]]
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[[Category: Padmanabhan, B.]]
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[[Category: Bessho Y]]
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[[Category: RSGI, RIKEN Structural Genomics/Proteomics Initiative.]]
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[[Category: Padmanabhan B]]
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[[Category: Yokoyama, S.]]
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[[Category: Yokoyama S]]
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[[Category: Alpha/beta/alpha sandwich structure]]
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[[Category: National project on protein structural and functional analyse]]
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[[Category: Nppsfa]]
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[[Category: Riken structural genomics/proteomics initiative]]
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[[Category: Rossman-type fold]]
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[[Category: Rsgi]]
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[[Category: Structural genomic]]
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[[Category: Transferase]]
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Current revision

Crystal structure of L-isoaspartyl protein carboxyl methyltranferase

PDB ID 2yxe

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