1u6r

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Current revision (06:39, 23 August 2023) (edit) (undo)
 
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<StructureSection load='1u6r' size='340' side='right'caption='[[1u6r]], [[Resolution|resolution]] 1.65&Aring;' scene=''>
<StructureSection load='1u6r' size='340' side='right'caption='[[1u6r]], [[Resolution|resolution]] 1.65&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[1u6r]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/European_rabbit European rabbit]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1U6R OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1U6R FirstGlance]. <br>
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<table><tr><td colspan='2'>[[1u6r]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1U6R OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1U6R FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=IOM:(DIAMINOMETHYL-METHYL-AMINO)-ACETIC+ACID'>IOM</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NO3:NITRATE+ION'>NO3</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.65&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1crk|1crk]]</div></td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=IOM:(DIAMINOMETHYL-METHYL-AMINO)-ACETIC+ACID'>IOM</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NO3:NITRATE+ION'>NO3</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CKM ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9986 European rabbit])</td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Creatine_kinase Creatine kinase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.3.2 2.7.3.2] </span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1u6r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1u6r OCA], [https://pdbe.org/1u6r PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1u6r RCSB], [https://www.ebi.ac.uk/pdbsum/1u6r PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1u6r 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=1u6r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1u6r OCA], [https://pdbe.org/1u6r PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1u6r RCSB], [https://www.ebi.ac.uk/pdbsum/1u6r PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1u6r ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/KCRM_RABIT KCRM_RABIT]] Reversibly catalyzes the transfer of phosphate between ATP and various phosphogens (e.g. creatine phosphate). Creatine kinase isoenzymes play a central role in energy transduction in tissues with large, fluctuating energy demands, such as skeletal muscle, heart, brain and spermatozoa.
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[https://www.uniprot.org/uniprot/KCRM_RABIT KCRM_RABIT] Reversibly catalyzes the transfer of phosphate between ATP and various phosphogens (e.g. creatine phosphate). Creatine kinase isoenzymes play a central role in energy transduction in tissues with large, fluctuating energy demands, such as skeletal muscle, heart, brain and spermatozoa.
== 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>
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[[Category: Creatine kinase]]
 
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[[Category: European rabbit]]
 
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Borders, C L]]
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[[Category: Oryctolagus cuniculus]]
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[[Category: Edmiston, P]]
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[[Category: Borders CL]]
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[[Category: Kundracik, M L]]
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[[Category: Edmiston P]]
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[[Category: Ohren, J F]]
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[[Category: Kundracik ML]]
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[[Category: Viola, R E]]
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[[Category: Ohren JF]]
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[[Category: Transferase]]
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[[Category: Viola RE]]

Current revision

Transition state analog complex of muscle creatine kinase (R134K) mutant

PDB ID 1u6r

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Proteopedia Page Contributors and Editors (what is this?)

OCA

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