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1z88

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Current revision (08:14, 25 October 2023) (edit) (undo)
 
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<StructureSection load='1z88' size='340' side='right'caption='[[1z88]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
<StructureSection load='1z88' size='340' side='right'caption='[[1z88]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[1z88]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Z88 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1Z88 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[1z88]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Salmonella_enterica_subsp._enterica_serovar_Typhimurium Salmonella enterica subsp. enterica serovar Typhimurium]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Z88 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1Z88 FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1z5g|1z5g]], [[1z5u|1z5u]]</div></td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Acid_phosphatase Acid phosphatase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.2 3.1.3.2] </span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1z88 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1z88 OCA], [https://pdbe.org/1z88 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1z88 RCSB], [https://www.ebi.ac.uk/pdbsum/1z88 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1z88 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=1z88 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1z88 OCA], [https://pdbe.org/1z88 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1z88 RCSB], [https://www.ebi.ac.uk/pdbsum/1z88 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1z88 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/APHA_SALTY APHA_SALTY]] Dephosphorylates several organic phosphate monoesters such as 3'-UMP, 5'-UMP and pNPP. 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 such as the 2'-, 3-, or 5'-hydroxyls of nucleosides and nucleotides. Also displays significant phosphomutase activity since it is able to catalyze the transfer of the phosphate group of 3'-AMP from the 3'-position both to the 2'- and 5'-positions. One of the physiological functions of the phosphohydrolytic activity of the enzyme is believed to be the scavenging of organic phosphate esters that otherwise cannot pass the cytoplasmic membrane.<ref>PMID:6256351</ref> <ref>PMID:3049613</ref>
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[https://www.uniprot.org/uniprot/APHA_SALTM APHA_SALTM] Dephosphorylates several organic phosphate monoesters. 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 (Probable).<ref>PMID:14501135</ref>
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</div>
</div>
<div class="pdbe-citations 1z88" style="background-color:#fffaf0;"></div>
<div class="pdbe-citations 1z88" style="background-color:#fffaf0;"></div>
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==See Also==
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*[[Acid phosphatase 3D structures|Acid phosphatase 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Acid phosphatase]]
 
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Gupta, G D]]
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[[Category: Salmonella enterica subsp. enterica serovar Typhimurium]]
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[[Category: Kumar, V]]
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[[Category: Gupta GD]]
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[[Category: Makde, R D]]
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[[Category: Kumar V]]
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[[Category: Class-b bacterial acid phosphatase]]
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[[Category: Makde RD]]
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[[Category: Hydrolase]]
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[[Category: Lys154arg mutant of mature apha]]
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[[Category: Metalloenzyme]]
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Current revision

Crystal structure of Lys154Arg mutant of mature AphA of S. typhimurium

PDB ID 1z88

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