1hfj: Difference between revisions

← Older edit

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-[[Image:1hfj.gif|left|200px]]
- {{Structure
+==Asparaginase from Erwinia chrysanthemi, hexagonal form with sulfate==
-|PDB= 1hfj |SIZE=350|CAPTION= <scene name='initialview01'>1hfj</scene>, resolution 2.40&Aring;
+<StructureSection load='1hfj' size='340' side='right'caption='[[1hfj]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
-|SITE= <scene name='pdbsite=AS1:Active+Site+Chain+A'>AS1</scene> and <scene name='pdbsite=AS2:Active+Site+Chain+C'>AS2</scene>
+== Structural highlights ==
-|LIGAND= <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene>
+<table><tr><td colspan='2'>[[1hfj]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Dickeya_chrysanthemi Dickeya chrysanthemi]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HFJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1HFJ FirstGlance]. <br>
-|ACTIVITY= [http://en.wikipedia.org/wiki/Asparaginase Asparaginase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.1.1 3.5.1.1]
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4&#8491;</td></tr>
-|GENE=
+<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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1hfj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hfj OCA], [https://pdbe.org/1hfj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1hfj RCSB], [https://www.ebi.ac.uk/pdbsum/1hfj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1hfj ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/ASPG_DICCH ASPG_DICCH]
+== Evolutionary Conservation ==
+[[Image:Consurf_key_small.gif|200px|right]]
+Check<jmol>
+  <jmolCheckbox>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/hf/1hfj_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+    <text>to colour the structure by Evolutionary Conservation</text>
+  </jmolCheckbox>
+</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1hfj ConSurf].
+<div style="clear:both"></div>
-'''ASPARAGINASE FROM ERWINIA CHRYSANTHEMI, HEXAGONAL FORM WITH SULFATE'''
+==See Also==
+*[[Asparaginase 3D structures|Asparaginase 3D structures]]
+__TOC__
-==Overview==
+</StructureSection>
-Quasi-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.
+[[Category: Dickeya chrysanthemi]]
+[[Category: Large Structures]]
-==About this Structure==
+[[Category: Jaskolski M]]
-HFJ is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Erwinia_chrysanthemi Erwinia chrysanthemi]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HFJ OCA].
+[[Category: Kozak M]]
+[[Category: Lubkowski J]]
-==Reference==
+[[Category: Palm GJ]]
-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:[http://www.ncbi.nlm.nih.gov/pubmed/11223513 11223513]
+[[Category: Wlodawer A]]
-[[Category: Asparaginase]]
-[[Category: Erwinia chrysanthemi]]
-[[Category: Single protein]]
-[[Category: Jaskolski, M.]]
-[[Category: Kozak, M.]]
-[[Category: Lubkowski, J.]]
-[[Category: Palm, G J.]]
-[[Category: Wlodawer, A.]]
-[[Category: SO4]]
-[[Category: hydrolase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:36:30 2008''