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[[Image:1qfx.jpg|left|200px]]
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{{STRUCTURE_1qfx|  PDB=1qfx  |  SCENE=  }}
'''PH 2.5 ACID PHOSPHATASE FROM ASPERGILLUS NIGER'''


==PH 2.5 ACID PHOSPHATASE FROM ASPERGILLUS NIGER==
<StructureSection load='1qfx' size='340' side='right'caption='[[1qfx]], [[Resolution|resolution]] 2.40&Aring;' 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]] 2.4&#8491;</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.


==Overview==
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>
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.


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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].
</div>
<div class="pdbe-citations 1qfx" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
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]
*[[Acid phosphatase 3D structures|Acid phosphatase 3D structures]]
[[Category: 3-phytase]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Aspergillus niger]]
[[Category: Aspergillus niger]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Arcy, A D.]]
[[Category: D'Arcy A]]
[[Category: Kostrewa, D.]]
[[Category: Kostrewa D]]
[[Category: Loon, A P.G M.Van.]]
[[Category: Van Loon APGM]]
[[Category: Wyss, M.]]
[[Category: Wyss M]]
[[Category: Phosphomonoesterase]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 06:13:16 2008''

Latest revision as of 23:47, 27 December 2023

PH 2.5 ACID PHOSPHATASE FROM ASPERGILLUS NIGER

1qfx, resolution 2.40Å

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