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[[Image:1q3k.png|left|200px]]


{{STRUCTURE_1q3k|  PDB=1q3k  |  SCENE=  }}
==Crystal structure of creatinine amidohydrolase (creatininase)==
 
<StructureSection load='1q3k' size='340' side='right'caption='[[1q3k]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
===Crystal structure of creatinine amidohydrolase (creatininase)===
== Structural highlights ==
 
<table><tr><td colspan='2'>[[1q3k]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_putida Pseudomonas putida]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Q3K OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1Q3K FirstGlance]. <br>
{{ABSTRACT_PUBMED_12946365}}
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1&#8491;</td></tr>
 
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
==About this Structure==
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1q3k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1q3k OCA], [https://pdbe.org/1q3k PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1q3k RCSB], [https://www.ebi.ac.uk/pdbsum/1q3k PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1q3k ProSAT]</span></td></tr>
[[1q3k]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Pseudomonas_putida Pseudomonas putida]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Q3K OCA].  
</table>
 
== Function ==
==Reference==
[https://www.uniprot.org/uniprot/CRNA_PSEPU CRNA_PSEPU] Cyclic amidohydrolase that catalyzes the reversible conversion of creatinine to creatine. Is also active toward glycocyamidine, though the reaction rate is very low, but it is completely inert toward hydantoin and its derivatives.<ref>PMID:500580</ref>  
<ref group="xtra">PMID:012946365</ref><references group="xtra"/>
== Evolutionary Conservation ==
[[Category: Creatininase]]
[[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/q3/1q3k_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=1q3k ConSurf].
<div style="clear:both"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Pseudomonas putida]]
[[Category: Pseudomonas putida]]
[[Category: Beuth, B.]]
[[Category: Beuth B]]
[[Category: Niefind, K.]]
[[Category: Niefind K]]
[[Category: Schomburg, D.]]
[[Category: Schomburg D]]
[[Category: Alpha-beta-fold]]
[[Category: Hydrolase]]

Latest revision as of 08:12, 14 February 2024

Crystal structure of creatinine amidohydrolase (creatininase)

1q3k, resolution 2.10Å

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