1z5u

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Current revision (08:14, 25 October 2023) (edit) (undo)
 
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<StructureSection load='1z5u' size='340' side='right'caption='[[1z5u]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
<StructureSection load='1z5u' size='340' side='right'caption='[[1z5u]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[1z5u]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Z5U OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1Z5U FirstGlance]. <br>
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<table><tr><td colspan='2'>[[1z5u]] 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=1Z5U OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1Z5U 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=CMP:ADENOSINE-3,5-CYCLIC-MONOPHOSPHATE'>CMP</scene>, <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]] 2.3&#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]], [[1z88|1z88]]</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=CMP:ADENOSINE-3,5-CYCLIC-MONOPHOSPHATE'>CMP</scene>, <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=1z5u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1z5u OCA], [https://pdbe.org/1z5u PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1z5u RCSB], [https://www.ebi.ac.uk/pdbsum/1z5u PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1z5u 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=1z5u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1z5u OCA], [https://pdbe.org/1z5u PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1z5u RCSB], [https://www.ebi.ac.uk/pdbsum/1z5u PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1z5u ProSAT]</span></td></tr>
</table>
</table>
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== Function ==
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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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</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=1z5u ConSurf].
</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=1z5u ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
 
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== Publication Abstract from PubMed ==
 
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The aphA gene of Salmonella enterica sv. Typhimurium strain MD6001 was cloned in the multicopy plasmid pBluescript SK(-). The recombinant AphA protein was purified to homogeneity. The protein crystallized in the orthorhombic space group P2(1)2(1)2(1), with unit-cell parameters a = 112.4, b = 130.2, c = 139.6 A. Consistent with the self-rotation function, there are two tetramers in the asymmetric unit, indicating a solvent content of approximately 54%. The crystals are composed of biologically active AphA molecules.
 
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Expression, purification, crystallization and preliminary X-ray diffraction studies of recombinant class B non-specific acid phosphatase of Salmonella typhimurium.,Makde RD, Kumar V, Gupta GD, Jasti J, Singh TP, Mahajan SK Acta Crystallogr D Biol Crystallogr. 2003 Oct;59(Pt 10):1849-52. Epub 2003, Sep 19. PMID:14501135<ref>PMID:14501135</ref>
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==See Also==
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*[[Acid phosphatase 3D structures|Acid phosphatase 3D structures]]
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 1z5u" style="background-color:#fffaf0;"></div>
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== 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: Kumar, V]]
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[[Category: Salmonella enterica subsp. enterica serovar Typhimurium]]
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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: Cyclic-amp complex of apha protein]]
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[[Category: Hydrolase]]
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[[Category: Metalloenzyme]]
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Current revision

Crystal structure of S. typhimurium AphA complexed with cyclic-AMP

PDB ID 1z5u

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