2yxe: Difference between revisions
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<StructureSection load='2yxe' size='340' side='right'caption='[[2yxe]], [[Resolution|resolution]] 2.00Å' scene=''> | <StructureSection load='2yxe' size='340' side='right'caption='[[2yxe]], [[Resolution|resolution]] 2.00Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2yxe]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/ | <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> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2Å</td></tr> | ||
<tr id=' | <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> | ||
<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> | <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> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[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]] | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: | [[Category: Methanocaldococcus jannaschii DSM 2661]] | ||
[[Category: Bessho | [[Category: Bessho Y]] | ||
[[Category: Padmanabhan | [[Category: Padmanabhan B]] | ||
[[Category: Yokoyama S]] | |||
[[Category: Yokoyama | |||
Latest revision as of 09:09, 25 October 2023
Crystal structure of L-isoaspartyl protein carboxyl methyltranferase
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