2b0c
From Proteopedia
(Difference between revisions)
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==The crystal structure of the putative phosphatase from Escherichia coli== | ==The crystal structure of the putative phosphatase from Escherichia coli== | ||
- | <StructureSection load='2b0c' size='340' side='right'caption='[[2b0c]]' scene=''> | + | <StructureSection load='2b0c' size='340' side='right'caption='[[2b0c]], [[Resolution|resolution]] 2.00Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
- | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2B0C OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2B0C FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2b0c]] is a 1 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=2B0C OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2B0C FirstGlance]. <br> |
- | </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=2b0c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2b0c OCA], [https://pdbe.org/2b0c PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2b0c RCSB], [https://www.ebi.ac.uk/pdbsum/2b0c PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2b0c ProSAT], [https://www.topsan.org/Proteins/MCSG/2b0c TOPSAN]</span></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]] 2Å</td></tr> |
+ | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=G1P:ALPHA-D-GLUCOSE-1-PHOSPHATE'>G1P</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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=2b0c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2b0c OCA], [https://pdbe.org/2b0c PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2b0c RCSB], [https://www.ebi.ac.uk/pdbsum/2b0c PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2b0c ProSAT], [https://www.topsan.org/Proteins/MCSG/2b0c TOPSAN]</span></td></tr> | ||
</table> | </table> | ||
+ | == Function == | ||
+ | [https://www.uniprot.org/uniprot/YIHX_ECOLI YIHX_ECOLI] Catalyzes the dephosphorylation of alpha-D-glucose-1-phosphate (Glu1P) and has no activity with the beta form. In addition, YihX has phosphatase activity against sugar-phosphate and pyridoxal phosphate (PLP) and low beta-phosphoglucomutase activity.<ref>PMID:15808744</ref> <ref>PMID:16990279</ref> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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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=2b0c 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=2b0c ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
+ | == References == | ||
+ | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
+ | [[Category: Escherichia coli K-12]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Edwards A]] | [[Category: Edwards A]] |
Revision as of 11:19, 22 May 2024
The crystal structure of the putative phosphatase from Escherichia coli
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