1qfx

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[[Image:1qfx.jpg|left|200px]]
 
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{{Structure
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==PH 2.5 ACID PHOSPHATASE FROM ASPERGILLUS NIGER==
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|PDB= 1qfx |SIZE=350|CAPTION= <scene name='initialview01'>1qfx</scene>, resolution 2.4&Aring;
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<StructureSection load='1qfx' size='340' side='right'caption='[[1qfx]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> and <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>
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<table><tr><td colspan='2'>[[1qfx]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Aspergillus_niger Aspergillus niger]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QFX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1QFX FirstGlance]. <br>
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|ACTIVITY= [http://en.wikipedia.org/wiki/3-phytase 3-phytase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.8 3.1.3.8]
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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]] 2.4&#8491;</td></tr>
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|GENE=
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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}}
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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=1qfx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qfx OCA], [https://pdbe.org/1qfx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1qfx RCSB], [https://www.ebi.ac.uk/pdbsum/1qfx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1qfx ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/PHYB_ASPAW PHYB_ASPAW] Catalyzes the hydrolysis of inorganic orthophosphate from phytate.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/qf/1qfx_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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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=1qfx ConSurf].
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<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 crystal structure of Aspergillus niger pH 2.5 acid phosphatase (EC 3.1.3.2) has been determined at 2.4 A resolution. In the crystal, two dimers form a tetramer in which the active sites are easily accessible to substrates. The main contacts in the dimer come from the N termini, each lying on the surface of the neighbouring molecule. The monomer consists of two domains, with the active site located at their interface. The active site has a highly conserved catalytic center and a charge distribution, which explains the highly acidic pH optimum and the broad substrate specificity of the enzyme.
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'''PH 2.5 ACID PHOSPHATASE FROM ASPERGILLUS NIGER'''
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Crystal structure of Aspergillus niger pH 2.5 acid phosphatase at 2. 4 A resolution.,Kostrewa D, Wyss M, D'Arcy A, van Loon AP J Mol Biol. 1999 May 21;288(5):965-74. PMID:10329192<ref>PMID:10329192</ref>
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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 1qfx" style="background-color:#fffaf0;"></div>
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==Overview==
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==See Also==
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The crystal structure of Aspergillus niger pH 2.5 acid phosphatase (EC 3.1.3.2) has been determined at 2.4 A resolution. In the crystal, two dimers form a tetramer in which the active sites are easily accessible to substrates. The main contacts in the dimer come from the N termini, each lying on the surface of the neighbouring molecule. The monomer consists of two domains, with the active site located at their interface. The active site has a highly conserved catalytic center and a charge distribution, which explains the highly acidic pH optimum and the broad substrate specificity of the enzyme.
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*[[Acid phosphatase 3D structures|Acid phosphatase 3D structures]]
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== References ==
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==About this Structure==
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<references/>
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1QFX is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Aspergillus_niger Aspergillus niger]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QFX OCA].
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__TOC__
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</StructureSection>
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==Reference==
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Crystal structure of Aspergillus niger pH 2.5 acid phosphatase at 2. 4 A resolution., Kostrewa D, Wyss M, D'Arcy A, van Loon AP, J Mol Biol. 1999 May 21;288(5):965-74. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10329192 10329192]
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[[Category: 3-phytase]]
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[[Category: Aspergillus niger]]
[[Category: Aspergillus niger]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Arcy, A D.]]
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[[Category: D'Arcy A]]
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[[Category: Kostrewa, D.]]
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[[Category: Kostrewa D]]
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[[Category: Loon, A P.G M.Van.]]
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[[Category: Van Loon APGM]]
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[[Category: Wyss, M.]]
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[[Category: Wyss M]]
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[[Category: GOL]]
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[[Category: NAG]]
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[[Category: SO4]]
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[[Category: phosphomonoesterase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:36:54 2008''
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Current revision

PH 2.5 ACID PHOSPHATASE FROM ASPERGILLUS NIGER

PDB ID 1qfx

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OCA

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