2bwj: Difference between revisions

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New page: left|200px<br /> <applet load="2bwj" size="450" color="white" frame="true" align="right" spinBox="true" caption="2bwj, resolution 2.30Å" /> '''STRUCTURE OF ADENYL...
 
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[[Image:2bwj.gif|left|200px]]<br />
<applet load="2bwj" size="450" color="white" frame="true" align="right" spinBox="true"
caption="2bwj, resolution 2.30&Aring;" />
'''STRUCTURE OF ADENYLATE KINASE 5'''<br />


==About this Structure==
==Structure of adenylate kinase 5==
2BWJ is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]] with SO4, CL and AMP as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[http://en.wikipedia.org/wiki/ ]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.4.3 2.7.4.3]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2BWJ OCA]].
<StructureSection load='2bwj' size='340' side='right'caption='[[2bwj]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2bwj]] is a 6 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=2BWJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2BWJ FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3&#8491;</td></tr>
<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=CL:CHLORIDE+ION'>CL</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=2bwj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bwj OCA], [https://pdbe.org/2bwj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2bwj RCSB], [https://www.ebi.ac.uk/pdbsum/2bwj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2bwj ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/KAD5_HUMAN KAD5_HUMAN] Nucleoside monophosphate (NMP) kinase that catalyzes the reversible transfer of the terminal phosphate group between nucleoside triphosphates and monophosphates. Active on AMP and dAMP with ATP as a donor. When GTP is used as phosphate donor, the enzyme phosphorylates AMP, CMP, and to a small extent dCMP. Also displays broad nucleoside diphosphate kinase activity.<ref>PMID:19647735</ref> <ref>PMID:23416111</ref>
== 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/bw/2bwj_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=2bwj ConSurf].
<div style="clear:both"></div>
 
==See Also==
*[[Adenylate kinase 3D structures|Adenylate kinase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Arrowsmith, C.]]
[[Category: Arrowsmith C]]
[[Category: Bunkoczi, G.]]
[[Category: Bunkoczi G]]
[[Category: Delft, F.Von.]]
[[Category: Edwards A]]
[[Category: Edwards, A.]]
[[Category: Fedorov O]]
[[Category: Fedorov, O.]]
[[Category: Filippakopoulos P]]
[[Category: Filippakopoulos, P.]]
[[Category: Jansson A]]
[[Category: Jansson, A.]]
[[Category: Knapp S]]
[[Category: Knapp, S.]]
[[Category: Longman E]]
[[Category: Longman, E.]]
[[Category: Sundstrom M]]
[[Category: Sundstrom, M.]]
[[Category: Ugochukwu E]]
[[Category: Ugochukwu, E.]]
[[Category: Weigelt J]]
[[Category: Weigelt, J.]]
[[Category: Von Delft F]]
[[Category: AMP]]
[[Category: CL]]
[[Category: SO4]]
[[Category: adenylate kinase]]
[[Category: phosphoryl transfer reaction]]
[[Category: transferase]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Oct 29 17:16:52 2007''

Latest revision as of 12:20, 9 May 2024

Structure of adenylate kinase 5Structure of adenylate kinase 5

Structural highlights

2bwj is a 6 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.3Å
Ligands:, ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

KAD5_HUMAN Nucleoside monophosphate (NMP) kinase that catalyzes the reversible transfer of the terminal phosphate group between nucleoside triphosphates and monophosphates. Active on AMP and dAMP with ATP as a donor. When GTP is used as phosphate donor, the enzyme phosphorylates AMP, CMP, and to a small extent dCMP. Also displays broad nucleoside diphosphate kinase activity.[1] [2]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

References

  1. ↑ Solaroli N, Panayiotou C, Johansson M, Karlsson A. Identification of two active functional domains of human adenylate kinase 5. FEBS Lett. 2009 Sep 3;583(17):2872-6. PMID:19647735 doi:10.1016/j.febslet.2009.07.047
  2. ↑ Amiri M, Conserva F, Panayiotou C, Karlsson A, Solaroli N. The human adenylate kinase 9 is a nucleoside mono Int J Biochem Cell Biol. 2013 May;45(5):925-31. PMID:23416111 doi:10.1016/j.biocel.2013.02.004

2bwj, resolution 2.30Å

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