2v5y
From Proteopedia
(Difference between revisions)
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<StructureSection load='2v5y' size='340' side='right'caption='[[2v5y]], [[Resolution|resolution]] 3.10Å' scene=''> | <StructureSection load='2v5y' size='340' side='right'caption='[[2v5y]], [[Resolution|resolution]] 3.10Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
- | <table><tr><td colspan='2'>[[2v5y]] is a 1 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[2v5y]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2V5Y OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2V5Y FirstGlance]. <br> |
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr> | ||
- | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1rpm|1rpm]], [[2c9a|2c9a]]</td></tr> | + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1rpm|1rpm]], [[2c9a|2c9a]]</div></td></tr> |
- | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Protein-tyrosine-phosphatase Protein-tyrosine-phosphatase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.48 3.1.3.48] </span></td></tr> |
- | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2v5y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2v5y OCA], [https://pdbe.org/2v5y PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2v5y RCSB], [https://www.ebi.ac.uk/pdbsum/2v5y PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2v5y ProSAT]</span></td></tr> |
</table> | </table> | ||
== Function == | == Function == | ||
- | [[ | + | [[https://www.uniprot.org/uniprot/PTPRM_HUMAN PTPRM_HUMAN]] Involved in cell-cell adhesion through homophilic interactions. May play a key role in signal transduction and growth control.<ref>PMID:16456543</ref> |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] |
Revision as of 12:39, 23 March 2022
Crystal structure of the receptor protein tyrosine phosphatase mu ectodomain
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Categories: Human | Large Structures | Protein-tyrosine-phosphatase | Aricescu, A R | Chang, V T | Choudhuri, K | Davis, S J | Jones, E Y | Lu, W | Merwe, P A.van der | Siebold, C | Cell adhesion | Extracellular region | Glycoprotein | Hydrolase | Immunoglobulin domain | Membrane | Protein phosphatase | Receptor | Receptor protein tyrosine phosphatase | Transmembrane