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2ak3
From Proteopedia
(Difference between revisions)
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<StructureSection load='2ak3' size='340' side='right'caption='[[2ak3]], [[Resolution|resolution]] 1.85Å' scene=''> | <StructureSection load='2ak3' size='340' side='right'caption='[[2ak3]], [[Resolution|resolution]] 1.85Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[2ak3]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/ | + | <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> |
| - | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.85Å</td></tr> |
| - | <tr id=' | + | <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> |
<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> | <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> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/KAD3_BOVIN KAD3_BOVIN] | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</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]. | </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> | <div style="clear:both"></div> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | 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. | ||
| - | |||
| - | 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:1994037<ref>PMID:1994037</ref> | ||
| - | |||
| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 2ak3" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
*[[Adenylate kinase 3D structures|Adenylate kinase 3D structures]] | *[[Adenylate kinase 3D structures|Adenylate kinase 3D structures]] | ||
| - | == References == | ||
| - | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Bos taurus]] |
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | + | [[Category: Diederichs K]] | |
| - | [[Category: Diederichs | + | [[Category: Schulz GE]] |
| - | [[Category: Schulz | + | |
Current revision
THE THREE-DIMENSIONAL STRUCTURE OF THE COMPLEX BETWEEN MITOCHONDRIAL MATRIX ADENYLATE KINASE AND ITS SUBSTRATE AMP AT 1.85 ANGSTROMS RESOLUTION
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