1hfk: Difference between revisions
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<StructureSection load='1hfk' size='340' side='right'caption='[[1hfk]], [[Resolution|resolution]] 2.17Å' scene=''> | <StructureSection load='1hfk' size='340' side='right'caption='[[1hfk]], [[Resolution|resolution]] 2.17Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1hfk]] is a 2 chain structure with sequence from [ | <table><tr><td colspan='2'>[[1hfk]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Erwinia_chrysanthemi Erwinia chrysanthemi]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HFK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1HFK FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3pga|3pga]], [[1hfj|1hfj]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3pga|3pga]], [[1hfj|1hfj]]</div></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/Asparaginase Asparaginase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.1.1 3.5.1.1] </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=1hfk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hfk OCA], [https://pdbe.org/1hfk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1hfk RCSB], [https://www.ebi.ac.uk/pdbsum/1hfk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1hfk ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
Revision as of 08:49, 28 April 2021
Asparaginase from Erwinia chrysanthemi, hexagonal form with weak sulfateAsparaginase from Erwinia chrysanthemi, hexagonal form with weak sulfate
Structural highlights
Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedQuasi-enantiomorphic crystals of the Y25F mutant of Escherichia coli L-asparaginase and of the native Erwinia chrysanthemi L-asparaginase were obtained in the hexagonal space groups P6(5)22 and P6(1)22, respectively. The structures of these highly homologous enzymes were solved by molecular replacement and were refined with data extending to 2.2-2.5 A. These structures were compared with each other, as well as with other L-asparaginase structures previously observed with different crystal packing. It is concluded that the observed phenomenon, which is rare, was most likely to have arisen by chance. Structures of two highly homologous bacterial L-asparaginases: a case of enantiomorphic space groups.,Jaskolski M, Kozak M, Lubkowski J, Palm G, Wlodawer A Acta Crystallogr D Biol Crystallogr. 2001 Mar;57(Pt 3):369-77. PMID:11223513[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences |
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