1kr5
From Proteopedia
(Difference between revisions)
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<StructureSection load='1kr5' size='340' side='right'caption='[[1kr5]], [[Resolution|resolution]] 2.10Å' scene=''> | <StructureSection load='1kr5' size='340' side='right'caption='[[1kr5]], [[Resolution|resolution]] 2.10Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[1kr5]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/ | + | <table><tr><td colspan='2'>[[1kr5]] is a 1 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=1KR5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1KR5 FirstGlance]. <br> |
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene></td></tr> | ||
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Protein-L-isoaspartate(D-aspartate)_O-methyltransferase Protein-L-isoaspartate(D-aspartate) O-methyltransferase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.77 2.1.1.77] </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=1kr5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kr5 OCA], [https://pdbe.org/1kr5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1kr5 RCSB], [https://www.ebi.ac.uk/pdbsum/1kr5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1kr5 ProSAT]</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=1kr5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kr5 OCA], [https://pdbe.org/1kr5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1kr5 RCSB], [https://www.ebi.ac.uk/pdbsum/1kr5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1kr5 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
| - | + | [https://www.uniprot.org/uniprot/PIMT_HUMAN PIMT_HUMAN] Catalyzes the methyl esterification of L-isoaspartyl and D-aspartyl 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. Acts on microtubule-associated protein 2, calreticulin, clathrin light chains a and b, Ubiquitin carboxyl-terminal hydrolase isozyme L1, phosphatidylethanolamine-binding protein 1, stathmin, beta-synuclein and alpha-synuclein (By similarity). | |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Homo sapiens]] |
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Clarke | + | [[Category: Clarke S]] |
| - | [[Category: Griffith | + | [[Category: Griffith SC]] |
| - | [[Category: MacLaren | + | [[Category: MacLaren DC]] |
| - | [[Category: Ryttersgaard | + | [[Category: Ryttersgaard C]] |
| - | [[Category: Sawaya | + | [[Category: Sawaya MR]] |
| - | [[Category: Yeates | + | [[Category: Yeates TO]] |
| - | + | ||
| - | + | ||
Revision as of 09:43, 21 December 2022
Crystal structure of human L-isoaspartyl methyltransferase
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