2heg
From Proteopedia
(Difference between revisions)
| Line 1: | Line 1: | ||
==Phospho-Aspartyl Intermediate Analogue of Apha class B acid phosphatase/phosphotransferase== | ==Phospho-Aspartyl Intermediate Analogue of Apha class B acid phosphatase/phosphotransferase== | ||
| - | <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 [ | + | <table><tr><td colspan='2'>[[2heg]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. 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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> |
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=BFD:ASPARTATE+BERYLLIUM+TRIFLUORIDE'>BFD</scene></td></tr> | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=BFD:ASPARTATE+BERYLLIUM+TRIFLUORIDE'>BFD</scene></td></tr> | ||
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2b82|2b82]], [[2g1a|2g1a]], [[1n9k|1n9k]], [[1rmy|1rmy]], [[2b8j|2b8j]], [[1rmq|1rmq]]</td></tr> | + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2b82|2b82]], [[2g1a|2g1a]], [[1n9k|1n9k]], [[1rmy|1rmy]], [[2b8j|2b8j]], [[1rmq|1rmq]]</div></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">aphA, napA ([ | + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">aphA, napA ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895])</td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Acid_phosphatase Acid phosphatase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.2 3.1.3.2] </span></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=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]] | ||
| Line 25: | Line 25: | ||
==See Also== | ==See Also== | ||
| - | *[[Acid phosphatase|Acid phosphatase]] | + | *[[Acid phosphatase 3D structures|Acid phosphatase 3D structures]] |
== References == | == References == | ||
<references/> | <references/> | ||
| Line 32: | Line 32: | ||
[[Category: Bacillus coli migula 1895]] | [[Category: Bacillus coli migula 1895]] | ||
[[Category: Acid phosphatase]] | [[Category: Acid phosphatase]] | ||
| + | [[Category: Large Structures]] | ||
[[Category: Benvenuti, M]] | [[Category: Benvenuti, M]] | ||
[[Category: Calderone, V]] | [[Category: Calderone, V]] | ||
Revision as of 07:37, 17 March 2021
Phospho-Aspartyl Intermediate Analogue of Apha class B acid phosphatase/phosphotransferase
| |||||||||||
