2hf2

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<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 ==
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<table><tr><td colspan='2'>[[2hf2]] is a 2 chain structure with sequence from [https://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 [https://proteopedia.org/fgij/fg.htm?mol=2HF2 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[2hf2]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. 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>
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</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>
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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]] 1.9&#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;'>[[1rlm|1rlm]], [[1rlo|1rlo]], [[1rlt|1rlt]]</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=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SupH ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</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/Sugar-phosphatase Sugar-phosphatase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.23 3.1.3.23] </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=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='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>
</table>
</table>
== Function ==
== Function ==
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[[https://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>
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[https://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]]
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Ecoli]]
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[[Category: Escherichia coli K-12]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Sugar-phosphatase]]
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[[Category: Almo SC]]
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[[Category: Almo, S C]]
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[[Category: Burley SK]]
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[[Category: Burley, S K]]
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[[Category: Patskovsky Y]]
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[[Category: Structural genomic]]
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[[Category: Ramagopal U]]
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[[Category: Patskovsky, Y]]
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[[Category: Ramagopal, U]]
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[[Category: Had family]]
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[[Category: Hydrolase]]
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[[Category: NYSGXRC, New York SGX Research Center for Structural Genomics]]
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[[Category: Phosphatase]]
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[[Category: PSI, Protein structure initiative]]
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Revision as of 09:57, 30 August 2023

Domain shifting confirms monomeric structure of Escherichia sugar phosphatase SUPH

PDB ID 2hf2

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