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==Domain shifting confirms monomeric structure of Escherichia sugar phosphatase SUPH==
==Domain shifting confirms monomeric structure of Escherichia sugar phosphatase SUPH==
<StructureSection load='2hf2' size='340' side='right' caption='[[2hf2]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
<StructureSection load='2hf2' size='340' side='right'caption='[[2hf2]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2hf2]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Ecoli Ecoli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HF2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2HF2 FirstGlance]. <br>
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HF2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2HF2 FirstGlance]. <br>
</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1rlm|1rlm]], [[1rlo|1rlo]], [[1rlt|1rlt]]</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SupH ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</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=2hf2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2hf2 OCA], [https://pdbe.org/2hf2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2hf2 RCSB], [https://www.ebi.ac.uk/pdbsum/2hf2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2hf2 ProSAT], [https://www.topsan.org/Proteins/NYSGXRC/2hf2 TOPSAN]</span></td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Sugar-phosphatase Sugar-phosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.23 3.1.3.23] </span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2hf2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2hf2 OCA], [http://pdbe.org/2hf2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2hf2 RCSB], [http://www.ebi.ac.uk/pdbsum/2hf2 PDBsum], [http://www.topsan.org/Proteins/NYSGXRC/2hf2 TOPSAN]</span></td></tr>
</table>
</table>
== Function ==
[[http://www.uniprot.org/uniprot/SUPH_ECOLI SUPH_ECOLI]] Catalyzes the hydrolysis of sugar phosphate to sugar and inorganic phosphate. Has a wide substrate specificity catalyzing the hydrolysis of ribose-5-phosphate, glucose-6-phosphate, fructose-1-phosphate, acetyl-phosphate, glycerol-1-phosphate, glycerol-2-phosphate, 2-deoxy-glucose-6-phosphate, mannose-6-phosphate and fructose-6-phosphate. Appears to have a low level of phosphotransferase activity using monophosphates as the phosphate donor.<ref>PMID:15808744</ref> <ref>PMID:16990279</ref> <ref>PMID:15657928</ref> 
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
Check<jmol>
   <jmolCheckbox>
   <jmolCheckbox>
     <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/hf/2hf2_consurf.spt"</scriptWhenChecked>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/hf/2hf2_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
   </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=2hf2 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=2hf2 ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Ecoli]]
[[Category: Large Structures]]
[[Category: Sugar-phosphatase]]
[[Category: Almo SC]]
[[Category: Almo, S C]]
[[Category: Burley SK]]
[[Category: Burley, S K]]
[[Category: Patskovsky Y]]
[[Category: Structural genomic]]
[[Category: Ramagopal U]]
[[Category: Patskovsky, Y]]
[[Category: Ramagopal, U]]
[[Category: Had family]]
[[Category: Hydrolase]]
[[Category: NYSGXRC, New York SGX Research Center for Structural Genomics]]
[[Category: Phosphatase]]
[[Category: PSI, Protein structure initiative]]

Latest revision as of 12:10, 6 November 2024

Domain shifting confirms monomeric structure of Escherichia sugar phosphatase SUPHDomain shifting confirms monomeric structure of Escherichia sugar phosphatase SUPH

Structural highlights

Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.9Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT, TOPSAN

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

2hf2, resolution 1.90Å

Drag the structure with the mouse to rotate

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OCA
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