1krm: Difference between revisions

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[[Image:1krm.png|left|200px]]


{{STRUCTURE_1krm| PDB=1krm | SCENE= }}
==Crystal structure of bovine adenosine deaminase complexed with 6-hydroxyl-1,6-dihydropurine riboside==
<StructureSection load='1krm' size='340' side='right'caption='[[1krm]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1krm]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KRM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1KRM FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PRH:6-HYDROXY-1,6-DIHYDRO+PURINE+NUCLEOSIDE'>PRH</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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=1krm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1krm OCA], [https://pdbe.org/1krm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1krm RCSB], [https://www.ebi.ac.uk/pdbsum/1krm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1krm ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/ADA_BOVIN ADA_BOVIN] Catalyzes the hydrolytic deamination of adenosine and 2-deoxyadenosine. Plays an important role in purine metabolism and in adenosine homeostasis. Modulates signaling by extracellular adenosine, and so contributes indirectly to cellular signaling events. Acts as a positive regulator of T-cell coactivation, by binding DPP4. Its interaction with DPP4 regulates lymphocyte-epithelial cell adhesion (By similarity).
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/kr/1krm_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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=1krm ConSurf].
<div style="clear:both"></div>


===Crystal structure of bovine adenosine deaminase complexed with 6-hydroxyl-1,6-dihydropurine riboside===
==See Also==
 
*[[Adenosine deaminase 3D structures|Adenosine deaminase 3D structures]]
{{ABSTRACT_PUBMED_12554940}}
__TOC__
 
</StructureSection>
==About this Structure==
[[1krm]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KRM OCA].
 
==Reference==
<ref group="xtra">PMID:012554940</ref><references group="xtra"/>
[[Category: Adenosine deaminase]]
[[Category: Bos taurus]]
[[Category: Bos taurus]]
[[Category: Kinoshita, T.]]
[[Category: Large Structures]]
[[Category: Adenosine deaminase]]
[[Category: Kinoshita T]]
[[Category: Hydrolase]]

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