2heg: Difference between revisions

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New page: left|200px<br /><applet load="2heg" size="350" color="white" frame="true" align="right" spinBox="true" caption="2heg, resolution 1.50Å" /> '''Phospho-Aspartyl Int...
 
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[[Image:2heg.jpg|left|200px]]<br /><applet load="2heg" size="350" color="white" frame="true" align="right" spinBox="true"
caption="2heg, resolution 1.50&Aring;" />
'''Phospho-Aspartyl Intermediate Analogue of Apha class B acid phosphatase/phosphotransferase'''<br />


==About this Structure==
==Phospho-Aspartyl Intermediate Analogue of Apha class B acid phosphatase/phosphotransferase==
2HEG 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 <scene name='pdbligand=MG:'>MG</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. 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] Known structural/functional Sites: <scene name='pdbsite=AC1:Mg+Binding+Site+For+Residue+A+300'>AC1</scene> and <scene name='pdbsite=AC2:Mg+Binding+Site+For+Residue+B+300'>AC2</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HEG OCA].  
<StructureSection load='2heg' size='340' side='right'caption='[[2heg]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
[[Category: Acid phosphatase]]
== Structural highlights ==
<table><tr><td colspan='2'>[[2heg]] 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=2HEG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2HEG 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]] 1.5&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BFD:ASPARTATE+BERYLLIUM+TRIFLUORIDE'>BFD</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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=2heg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2heg OCA], [https://pdbe.org/2heg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2heg RCSB], [https://www.ebi.ac.uk/pdbsum/2heg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2heg 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/he/2heg_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=2heg 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: Cappelletti, E.]]
[[Category: Cappelletti E]]
[[Category: Leone, R.]]
[[Category: Leone R]]
[[Category: Mangani, S.]]
[[Category: Mangani S]]
[[Category: MG]]
[[Category: apha class b acid phosphatase/phosphotransferase]]
[[Category: hydrolase]]
 
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