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3b6r

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Current revision (14:42, 1 November 2023) (edit) (undo)
 
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<StructureSection load='3b6r' size='340' side='right'caption='[[3b6r]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
<StructureSection load='3b6r' size='340' side='right'caption='[[3b6r]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3b6r]] is a 2 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=3B6R OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3B6R FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3b6r]] 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=3B6R OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3B6R 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=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=CRN:N-[(E)-AMINO(IMINO)METHYL]-N-METHYLGLYCINE'>CRN</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]] 2&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CKB ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=CRN:N-[(E)-AMINO(IMINO)METHYL]-N-METHYLGLYCINE'>CRN</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='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=3b6r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3b6r OCA], [https://pdbe.org/3b6r PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3b6r RCSB], [https://www.ebi.ac.uk/pdbsum/3b6r PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3b6r 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=3b6r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3b6r OCA], [https://pdbe.org/3b6r PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3b6r RCSB], [https://www.ebi.ac.uk/pdbsum/3b6r PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3b6r ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/KCRB_HUMAN KCRB_HUMAN]] 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/KCRB_HUMAN KCRB_HUMAN] 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: Homo sapiens]]
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[[Category: Human]]
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[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Bong, S M]]
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[[Category: Bong SM]]
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[[Category: Hwang, K Y]]
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[[Category: Hwang KY]]
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[[Category: Moon, J H]]
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[[Category: Moon JH]]
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[[Category: Atp-binding]]
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[[Category: Brain type]]
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[[Category: Cytoplasm]]
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[[Category: Dimeric]]
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[[Category: Kinase]]
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[[Category: Nucleotide-binding]]
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[[Category: Phosphorylation]]
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[[Category: Polymorphism]]
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[[Category: Transferase]]
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Current revision

Crystal structure of Human Brain-type Creatine Kinase

PDB ID 3b6r

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OCA

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