1rkq
From Proteopedia
(Difference between revisions)
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<StructureSection load='1rkq' size='340' side='right'caption='[[1rkq]], [[Resolution|resolution]] 1.40Å' scene=''> | <StructureSection load='1rkq' size='340' side='right'caption='[[1rkq]], [[Resolution|resolution]] 1.40Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[1rkq]] is a 2 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[1rkq]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RKQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1RKQ FirstGlance]. <br> |
| - | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.4Å</td></tr> |
| - | <tr id=' | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</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'>[ | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1rkq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rkq OCA], [https://pdbe.org/1rkq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1rkq RCSB], [https://www.ebi.ac.uk/pdbsum/1rkq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1rkq ProSAT], [https://www.topsan.org/Proteins/NYSGXRC/1rkq TOPSAN]</span></td></tr> |
</table> | </table> | ||
== Function == | == Function == | ||
| - | [ | + | [https://www.uniprot.org/uniprot/YIDA_ECOLI YIDA_ECOLI] Catalyzes the dephosphorylation of different sugar phosphates including erythrose-4-phosphate (Ery4P), ribose-5-phosphate (Ribu5P), fructose-1-phosphate (Fru1P), fructose-6-phosphate (Fru6P), glucose-6-P (Glu6P), and also imidodiphosphate (Imido-di-P) and acetyl phosphate (Acetyl-P). Selectively hydrolyzes alpha-D-glucose-1-phosphate (Glu1P) and has no activity with the beta form.<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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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Escherichia coli]] |
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Almo | + | [[Category: Almo SC]] |
| - | [[Category: Burley | + | [[Category: Burley SK]] |
| - | + | [[Category: Ramagopal UA]] | |
| - | [[Category: Ramagopal | + | |
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Current revision
Crystal structure of HAD-like phosphatase yidA from E. coli
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