2heg
From Proteopedia
(Difference between revisions)
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<StructureSection load='2heg' size='340' side='right'caption='[[2heg]], [[Resolution|resolution]] 1.50Å' scene=''> | <StructureSection load='2heg' size='340' side='right'caption='[[2heg]], [[Resolution|resolution]] 1.50Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
- | <table><tr><td colspan='2'>[[2heg]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/ | + | <table><tr><td colspan='2'>[[2heg]] 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=2HEG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2HEG 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]] 1.5Å</td></tr> |
- | <tr id=' | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BFD:ASPARTATE+BERYLLIUM+TRIFLUORIDE'>BFD</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></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=2heg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2heg OCA], [https://pdbe.org/2heg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2heg RCSB], [https://www.ebi.ac.uk/pdbsum/2heg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2heg ProSAT]</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=2heg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2heg OCA], [https://pdbe.org/2heg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2heg RCSB], [https://www.ebi.ac.uk/pdbsum/2heg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2heg ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
- | + | [https://www.uniprot.org/uniprot/APHA_ECOLI APHA_ECOLI] Dephosphorylates several organic phosphate monoesters including 3'- and 5'-nucleotides, 2'-deoxy-5'-nucleotides, pNPP, phenyl phosphate, glycerol 2-phosphate, ribose 5-phosphate, O-phospho-L-amino acids and phytic acid, showing the highest activity with aryl phosphoesters (pNPP, phenyl phosphate and O-phospho-L-tyrosine), and to a lesser extent with 3'- and 5'-nucleotides. No activity toward ATP, phosphodiesters, glycerol-1-phosphate, glucose 1-phosphate, glucose 6-phosphate, NADP, GTP or 3',5'-cAMP, ADP or ATP. Also has a phosphotransferase activity catalyzing the transfer of low-energy phosphate groups from organic phosphate monoesters to free hydroxyl groups of various organic compounds. Capable of transferring phosphate from either pNPP or UMP to adenosine or uridine. Does not exhibit nucleotide phosphomutase activity.<ref>PMID:9011040</ref> <ref>PMID:16297670</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]] |
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[[Category: Large Structures]] | [[Category: Large Structures]] | ||
- | [[Category: Benvenuti | + | [[Category: Benvenuti M]] |
- | [[Category: Calderone | + | [[Category: Calderone V]] |
- | [[Category: Cappelletti | + | [[Category: Cappelletti E]] |
- | [[Category: Leone | + | [[Category: Leone R]] |
- | [[Category: Mangani | + | [[Category: Mangani S]] |
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Current revision
Phospho-Aspartyl Intermediate Analogue of Apha class B acid phosphatase/phosphotransferase
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