1rmq: Difference between revisions

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New page: left|200px<br /><applet load="1rmq" size="450" color="white" frame="true" align="right" spinBox="true" caption="1rmq, resolution 2.00Å" /> '''Crystal structure of...
 
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[[Image:1rmq.jpg|left|200px]]<br /><applet load="1rmq" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1rmq, resolution 2.00&Aring;" />
'''Crystal structure of AphA class B acid phosphatase/phosphotransferase with osmiate mimicking the catalytic intermediate'''<br />


==About this Structure==
==Crystal structure of AphA class B acid phosphatase/phosphotransferase with osmiate mimicking the catalytic intermediate==
1RMQ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with CO and OS as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Acid_phosphatase Acid phosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.2 3.1.3.2] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1RMQ OCA].  
<StructureSection load='1rmq' size='340' side='right'caption='[[1rmq]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
[[Category: Acid phosphatase]]
== Structural highlights ==
<table><tr><td colspan='2'>[[1rmq]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RMQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1RMQ 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&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CO:COBALT+(II)+ION'>CO</scene>, <scene name='pdbligand=OS:OSMIUM+ION'>OS</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=1rmq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rmq OCA], [https://pdbe.org/1rmq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1rmq RCSB], [https://www.ebi.ac.uk/pdbsum/1rmq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1rmq ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/APHA_ECOLI APHA_ECOLI] Dephosphorylates several organic phosphate monoesters including 3'- and 5'-nucleotides, 2'-deoxy-5'-nucleotides, pNPP, phenyl phosphate, glycerol 2-phosphate, ribose 5-phosphate, O-phospho-L-amino acids and phytic acid, showing the highest activity with aryl phosphoesters (pNPP, phenyl phosphate and O-phospho-L-tyrosine), and to a lesser extent with 3'- and 5'-nucleotides. No activity toward ATP, phosphodiesters, glycerol-1-phosphate, glucose 1-phosphate, glucose 6-phosphate, NADP, GTP or 3',5'-cAMP, ADP or ATP. Also has a phosphotransferase activity catalyzing the transfer of low-energy phosphate groups from organic phosphate monoesters to free hydroxyl groups of various organic compounds. Capable of transferring phosphate from either pNPP or UMP to adenosine or uridine. Does not exhibit nucleotide phosphomutase activity.<ref>PMID:9011040</ref> <ref>PMID:16297670</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/rm/1rmq_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=1rmq ConSurf].
<div style="clear:both"></div>
 
==See Also==
*[[Acid phosphatase 3D structures|Acid phosphatase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Benvenuti, M.]]
[[Category: Benvenuti M]]
[[Category: Calderone, V.]]
[[Category: Calderone V]]
[[Category: Forleo, C.]]
[[Category: Forleo C]]
[[Category: Mangani, S.]]
[[Category: Mangani S]]
[[Category: Rossolini, G.M.]]
[[Category: Rossolini GM]]
[[Category: Thaller, M.C.]]
[[Category: Thaller MC]]
[[Category: CO]]
[[Category: OS]]
[[Category: class b acid phosphatase]]
[[Category: dddd acid phosphatase]]
[[Category: metallo-enzyme]]
[[Category: osmiate]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 01:43:02 2007''
Retrieved from "https://proteopedia.org/1rmq"