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[[Image:2ak3.gif|left|200px]]


{{Structure
==THE THREE-DIMENSIONAL STRUCTURE OF THE COMPLEX BETWEEN MITOCHONDRIAL MATRIX ADENYLATE KINASE AND ITS SUBSTRATE AMP AT 1.85 ANGSTROMS RESOLUTION==
|PDB= 2ak3 |SIZE=350|CAPTION= <scene name='initialview01'>2ak3</scene>, resolution 1.85&Aring;
<StructureSection load='2ak3' size='340' side='right'caption='[[2ak3]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND= <scene name='pdbligand=AMP:ADENOSINE+MONOPHOSPHATE'>AMP</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>
<table><tr><td colspan='2'>[[2ak3]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1ak3 1ak3]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2AK3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2AK3 FirstGlance]. <br>
|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Nucleoside-triphosphate--adenylate_kinase Nucleoside-triphosphate--adenylate kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.4.10 2.7.4.10] </span>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.85&#8491;</td></tr>
|GENE=
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AMP:ADENOSINE+MONOPHOSPHATE'>AMP</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
|DOMAIN=
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2ak3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ak3 OCA], [https://pdbe.org/2ak3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ak3 RCSB], [https://www.ebi.ac.uk/pdbsum/2ak3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ak3 ProSAT]</span></td></tr>
|RELATEDENTRY=
</table>
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ak3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ak3 OCA], [http://www.ebi.ac.uk/pdbsum/2ak3 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2ak3 RCSB]</span>
== Function ==
}}
[https://www.uniprot.org/uniprot/KAD3_BOVIN KAD3_BOVIN]
== 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/ak/2ak3_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=2ak3 ConSurf].
<div style="clear:both"></div>


'''THE THREE-DIMENSIONAL STRUCTURE OF THE COMPLEX BETWEEN MITOCHONDRIAL MATRIX ADENYLATE KINASE AND ITS SUBSTRATE AMP AT 1.85 ANGSTROMS RESOLUTION'''
==See Also==
 
*[[Adenylate kinase 3D structures|Adenylate kinase 3D structures]]
 
__TOC__
==Overview==
</StructureSection>
The crystal structure of the complex between adenylate kinase from bovine mitochondrial matrix and its substrate AMP has been refined at 1.85 A resolution (1 A = 0.1 nm). Based on 42,519 independent reflections of better than 10 A resolution, a final R-factor of 18.9% was obtained with a model obeying standard geometry within 0.016 A in bond lengths and 3.2 degrees in bond angles. There are two enzyme: substrate complexes in the asymmetric unit, each consisting of 226 amino acid residues, one AMP and one sulfate ion. A superposition of the two full-length polypeptides revealed deviations that can be described as small relative movements of three domains. Best superpositions of individual domains yielded a residual overall root-mean-square deviation of 0.3 A for the backbone atoms and 0.5 A for the sidechains. The final model contains 381 solvent molecules in the asymmetric unit, 2 x 72 = 144 of which occupy corresponding positions in both complexes.
 
==About this Structure==
2AK3 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. This structure supersedes the now removed PDB entry 1AK3. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2AK3 OCA].
 
==Reference==
The refined structure of the complex between adenylate kinase from beef heart mitochondrial matrix and its substrate AMP at 1.85 A resolution., Diederichs K, Schulz GE, J Mol Biol. 1991 Feb 5;217(3):541-9. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/1994037 1994037]
[[Category: Bos taurus]]
[[Category: Bos taurus]]
[[Category: Nucleoside-triphosphate--adenylate kinase]]
[[Category: Large Structures]]
[[Category: Single protein]]
[[Category: Diederichs K]]
[[Category: Diederichs, K.]]
[[Category: Schulz GE]]
[[Category: Schulz, G E.]]
[[Category: transferase (phosphotransferase)]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 01:53:46 2008''
Retrieved from "https://proteopedia.org/2ak3"