4qak
From Proteopedia
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4qak]] 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=4QAK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4QAK FirstGlance]. <br> | <table><tr><td colspan='2'>[[4qak]] 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=4QAK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4QAK FirstGlance]. <br> | ||
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=2AM:ADENOSINE-2-MONOPHOSPHATE'>2AM</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></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]] 2.025Å</td></tr> |
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=2AM:ADENOSINE-2-MONOPHOSPHATE'>2AM</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</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=4qak FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4qak OCA], [https://pdbe.org/4qak PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4qak RCSB], [https://www.ebi.ac.uk/pdbsum/4qak PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4qak 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=4qak FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4qak OCA], [https://pdbe.org/4qak PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4qak RCSB], [https://www.ebi.ac.uk/pdbsum/4qak PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4qak ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
| - | [https://www.uniprot.org/uniprot/THPR_ECOLI THPR_ECOLI] Hydrolyzes RNA 2',3'-cyclic phosphodiester to an RNA 2'-phosphomonoester (PubMed:25239919). In vitro, can also ligate 5' and 3' half-tRNA molecules with 2',3'-cyclic phosphate and 5'-hydroxyl termini, respectively, to the product containing the 2'-5' phosphodiester linkage. This reaction does not require ATP and is reversible (PubMed:6347395 | + | [https://www.uniprot.org/uniprot/THPR_ECOLI THPR_ECOLI] Hydrolyzes RNA 2',3'-cyclic phosphodiester to an RNA 2'-phosphomonoester (PubMed:25239919). In vitro, can also ligate 5' and 3' half-tRNA molecules with 2',3'-cyclic phosphate and 5'-hydroxyl termini, respectively, to the product containing the 2'-5' phosphodiester linkage. This reaction does not require ATP and is reversible (PubMed:6347395, PubMed:8940112).<ref>PMID:25239919</ref> <ref>PMID:6347395</ref> <ref>PMID:8940112</ref> |
==See Also== | ==See Also== | ||
Current revision
Crystal structure of phosphoesterase
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