1rmy: Difference between revisions

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New page: left|200px<br /><applet load="1rmy" size="450" color="white" frame="true" align="right" spinBox="true" caption="1rmy, resolution 1.75Å" /> '''Crystal structure of...
 
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[[Image:1rmy.gif|left|200px]]<br /><applet load="1rmy" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1rmy, resolution 1.75&Aring;" />
'''Crystal structure of AphA class B acid phosphatase/phosphotransferase ternary complex with deoxycytosine and phosphate bound to the catalytic metal'''<br />


==About this Structure==
==Crystal structure of AphA class B acid phosphatase/phosphotransferase ternary complex with deoxycytosine and phosphate bound to the catalytic metal==
1RMY 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 MG, PO4 and DCZ 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=1RMY OCA].  
<StructureSection load='1rmy' size='340' side='right'caption='[[1rmy]], [[Resolution|resolution]] 1.75&Aring;' scene=''>
[[Category: Acid phosphatase]]
== Structural highlights ==
<table><tr><td colspan='2'>[[1rmy]] 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=1RMY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1RMY 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]] 1.75&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DCZ:2-DEOXYCYTIDINE'>DCZ</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</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=1rmy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rmy OCA], [https://pdbe.org/1rmy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1rmy RCSB], [https://www.ebi.ac.uk/pdbsum/1rmy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1rmy 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/1rmy_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=1rmy 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: DCZ]]
[[Category: MG]]
[[Category: PO4]]
[[Category: class b acid phosphatase]]
[[Category: dcmp]]
[[Category: dddd acid phosphatase]]
[[Category: metallo-enzyme]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 01:43:23 2007''