1qfx
From Proteopedia
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| - | [[Image:1qfx.jpg|left|200px]]<br /><applet load="1qfx" size="350" color="white" frame="true" align="right" spinBox="true" | ||
| - | caption="1qfx, resolution 2.4Å" /> | ||
| - | '''PH 2.5 ACID PHOSPHATASE FROM ASPERGILLUS NIGER'''<br /> | ||
| - | == | + | ==PH 2.5 ACID PHOSPHATASE FROM ASPERGILLUS NIGER== |
| + | <StructureSection load='1qfx' size='340' side='right'caption='[[1qfx]], [[Resolution|resolution]] 2.40Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <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> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4Å</td></tr> | ||
| + | <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> | ||
| + | <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> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/PHYB_ASPAW PHYB_ASPAW] Catalyzes the hydrolysis of inorganic orthophosphate from phytate. | ||
| + | == 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/qf/1qfx_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=1qfx ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
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. | 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. | ||
| - | + | 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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 1qfx" style="background-color:#fffaf0;"></div> | |
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| - | + | ==See Also== | |
| + | *[[Acid phosphatase 3D structures|Acid phosphatase 3D structures]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Aspergillus niger]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: D'Arcy A]] | ||
| + | [[Category: Kostrewa D]] | ||
| + | [[Category: Van Loon APGM]] | ||
| + | [[Category: Wyss M]] | ||
Current revision
PH 2.5 ACID PHOSPHATASE FROM ASPERGILLUS NIGER
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