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2cdn

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<StructureSection load='2cdn' size='340' side='right'caption='[[2cdn]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
<StructureSection load='2cdn' size='340' side='right'caption='[[2cdn]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[2cdn]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Myctu Myctu]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CDN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2CDN FirstGlance]. <br>
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<table><tr><td colspan='2'>[[2cdn]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycobacterium_tuberculosis_H37Rv Mycobacterium tuberculosis H37Rv]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CDN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2CDN FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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]] 1.9&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1p4s|1p4s]]</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=MG:MAGNESIUM+ION'>MG</scene></td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Adenylate_kinase Adenylate kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.4.3 2.7.4.3] </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=2cdn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2cdn OCA], [https://pdbe.org/2cdn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2cdn RCSB], [https://www.ebi.ac.uk/pdbsum/2cdn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2cdn ProSAT]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2cdn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2cdn OCA], [http://pdbe.org/2cdn PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2cdn RCSB], [http://www.ebi.ac.uk/pdbsum/2cdn PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2cdn ProSAT]</span></td></tr>
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</table>
</table>
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== Function ==
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[https://www.uniprot.org/uniprot/KAD_MYCTU KAD_MYCTU] Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. This small ubiquitous enzyme involved in the energy metabolism and nucleotide synthesis, is essential for maintenance and cell growth. Has a broad specificity for nucleoside triphosphates, being highly active with ATP or dATP as phosphate donors, and less active with GTP or UTP.<ref>PMID:10398370</ref>
== 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: Adenylate kinase]]
 
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Myctu]]
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[[Category: Mycobacterium tuberculosis H37Rv]]
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[[Category: Alzari, P M]]
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[[Category: Alzari PM]]
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[[Category: Bellinzoni, M]]
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[[Category: Bellinzoni M]]
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[[Category: Grana, M]]
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[[Category: Grana M]]
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[[Category: Haouz, A]]
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[[Category: Haouz A]]
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[[Category: Munier-Lehmann, H]]
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[[Category: Munier-Lehmann H]]
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[[Category: Associative mechanism]]
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[[Category: Atp-binding]]
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[[Category: Kinase]]
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[[Category: Nucleotide biosynthesis]]
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[[Category: Nucleotide-binding]]
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[[Category: Phosphoryl transfer]]
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[[Category: Transferase]]
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Current revision

Crystal structure of Mycobacterium tuberculosis adenylate kinase complexed with two molecules of ADP and Mg

PDB ID 2cdn

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