5yf0: Difference between revisions

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<StructureSection load='5yf0' size='340' side='right'caption='[[5yf0]], [[Resolution|resolution]] 2.25&Aring;' scene=''>
<StructureSection load='5yf0' size='340' side='right'caption='[[5yf0]], [[Resolution|resolution]] 2.25&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[5yf0]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5YF0 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5YF0 FirstGlance]. <br>
<table><tr><td colspan='2'>[[5yf0]] 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=5YF0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5YF0 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=SAM:S-ADENOSYLMETHIONINE'>SAM</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.25&#8491;</td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Carnosine_N-methyltransferase Carnosine N-methyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.22 2.1.1.22] </span></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=SAM:S-ADENOSYLMETHIONINE'>SAM</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5yf0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5yf0 OCA], [http://pdbe.org/5yf0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5yf0 RCSB], [http://www.ebi.ac.uk/pdbsum/5yf0 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5yf0 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=5yf0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5yf0 OCA], [https://pdbe.org/5yf0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5yf0 RCSB], [https://www.ebi.ac.uk/pdbsum/5yf0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5yf0 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/CARME_HUMAN CARME_HUMAN]] N-methyltransferase that mediates the formation of anserine (beta-alanyl-N(Pi)-methyl-L-histidine) from carnosine. Anserine, a methylated derivative of carnosine (beta-alanyl-L-histidine), is an abundant constituent of vertebrate skeletal muscles. Also methylates other L-histidine-containing di- and tripeptides such as Gly-Gly-His, Gly-His and homocarnosine (GABA-His).<ref>PMID:26001783</ref>
[https://www.uniprot.org/uniprot/CARME_HUMAN CARME_HUMAN] N-methyltransferase that mediates the formation of anserine (beta-alanyl-N(Pi)-methyl-L-histidine) from carnosine. Anserine, a methylated derivative of carnosine (beta-alanyl-L-histidine), is an abundant constituent of vertebrate skeletal muscles. Also methylates other L-histidine-containing di- and tripeptides such as Gly-Gly-His, Gly-His and homocarnosine (GABA-His).<ref>PMID:26001783</ref>  
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Carnosine N-methyltransferase]]
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Cao, R]]
[[Category: Cao R]]
[[Category: Li, H]]
[[Category: Li H]]
[[Category: Zhang, X]]
[[Category: Zhang X]]
[[Category: Complex]]
[[Category: Methyltransferase]]
[[Category: Sam]]
[[Category: Transferase]]

Latest revision as of 10:23, 27 March 2024

Crystal structure of CARNMT1 bound to SAM

5yf0, resolution 2.25Å

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