View source for 2c95


==Structure of adenylate kinase 1 in complex with P1,P4-di(adenosine) tetraphosphate==
<StructureSection load='2c95' size='340' side='right'caption='[[2c95]], [[Resolution|resolution]] 1.71&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2c95]] 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=2C95 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2C95 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=B4P:BIS(ADENOSINE)-5-TETRAPHOSPHATE'>B4P</scene>, <scene name='pdbligand=MLI:MALONATE+ION'>MLI</scene></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1z83|1z83]]</div></td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Adenylate_kinase Adenylate kinase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.4.3 2.7.4.3] </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=2c95 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2c95 OCA], [https://pdbe.org/2c95 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2c95 RCSB], [https://www.ebi.ac.uk/pdbsum/2c95 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2c95 ProSAT]</span></td></tr>
</table>
== Disease ==
[[https://www.uniprot.org/uniprot/KAD1_HUMAN KAD1_HUMAN]] Defects in AK1 are the cause of hemolytic anemia due to adenylate kinase deficiency (HAAKD) [MIM:[https://omim.org/entry/612631 612631]].<ref>PMID:2542324</ref> <ref>PMID:9432020</ref> <ref>PMID:12649162</ref>  
== Function ==
[[https://www.uniprot.org/uniprot/KAD1_HUMAN KAD1_HUMAN]] Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Small ubiquitous enzyme involved in energy metabolism and nucleotide synthesis that is essential for maintenance and cell growth. 
== 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/c9/2c95_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=2c95 ConSurf].
<div style="clear:both"></div>

==See Also==
*[[Adenylate kinase 3D structures|Adenylate kinase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Adenylate kinase]]
[[Category: Human]]
[[Category: Large Structures]]
[[Category: Arrowsmith, C]]
[[Category: Bunkoczi, G]]
[[Category: Delft, F von]]
[[Category: Edwards, A]]
[[Category: Filippakopoulos, P]]
[[Category: Jansson, A]]
[[Category: Knapp, S]]
[[Category: Longman, E]]
[[Category: Sundstrom, M]]
[[Category: Ap4a]]
[[Category: Nucleotide kinase]]
[[Category: Transferase]]
[[Category: Transferase atp-binding]]