4d96: Difference between revisions

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 ==D-Cysteine desulfhydrase from Salmonella typhimurium complexed with 1-amino-1-carboxycyclopropane (ACC)==
-<StructureSection load='4d96' size='340' side='right' caption='[[4d96]], [[Resolution|resolution]] 2.09&Aring;' scene=''>
+<StructureSection load='4d96' size='340' side='right'caption='[[4d96]], [[Resolution|resolution]] 2.09&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[4d96]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_typhimurium"_loeffler_1892 "bacillus typhimurium" loeffler 1892]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4D96 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4D96 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[4d96]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Salmonella_enterica_subsp._enterica_serovar_Typhimurium Salmonella enterica subsp. enterica serovar Typhimurium]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4D96 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4D96 FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=5PA:N-[3-HYDROXY-2-METHYL-5-PHOSPHONOOXYMETHYL-PYRIDIN-4-Y-LMETHYL]-1-AMINO-CYCLOPROPANECARBOXYLIC+ACID'>5PA</scene>, <scene name='pdbligand=BEN:BENZAMIDINE'>BEN</scene>, <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=5PA:N-[3-HYDROXY-2-METHYL-5-PHOSPHONOOXYMETHYL-PYRIDIN-4-Y-LMETHYL]-1-AMINO-CYCLOPROPANECARBOXYLIC+ACID'>5PA</scene>, <scene name='pdbligand=BEN:BENZAMIDINE'>BEN</scene>, <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">[[4d8t|4d8t]], [[4d8u|4d8u]], [[4d8w|4d8w]], [[4d92|4d92]], [[4d97|4d97]], [[4d99|4d99]], [[4d9b|4d9b]], [[4d9c|4d9c]], [[4d9e|4d9e]], [[4d9f|4d9f]]</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=4d96 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4d96 OCA], [https://pdbe.org/4d96 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4d96 RCSB], [https://www.ebi.ac.uk/pdbsum/4d96 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4d96 ProSAT]</span></td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">dcyD, STM1953 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=90371 "Bacillus typhimurium" Loeffler 1892])</td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/D-cysteine_desulfhydrase D-cysteine desulfhydrase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.4.1.15 4.4.1.15] </span></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4d96 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4d96 OCA], [http://pdbe.org/4d96 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4d96 RCSB], [http://www.ebi.ac.uk/pdbsum/4d96 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4d96 ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/DCYD_SALTY DCYD_SALTY]] Catalyzes the alpha,beta-elimination reaction of D-cysteine and of several D-cysteine derivatives. It could be a defense mechanism against D-cysteine.[HAMAP-Rule:MF_01045]
+[[https://www.uniprot.org/uniprot/DCYD_SALTY DCYD_SALTY]] Catalyzes the alpha,beta-elimination reaction of D-cysteine and of several D-cysteine derivatives. It could be a defense mechanism against D-cysteine.[HAMAP-Rule:MF_01045]
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 25: / Line 22: @@
 __TOC__
 </StructureSection>
-[[Category: Bacillus typhimurium loeffler 1892]]
+[[Category: Large Structures]]
-[[Category: D-cysteine desulfhydrase]]
+[[Category: Salmonella enterica subsp. enterica serovar Typhimurium]]
-[[Category: Bharath, S R]]
+[[Category: Bharath SR]]
-[[Category: Murthy, M R.N]]
+[[Category: Murthy MRN]]
-[[Category: Rajesh, K H]]
+[[Category: Rajesh KH]]
-[[Category: Savithri, H S]]
+[[Category: Savithri HS]]
-[[Category: Shveta, B]]
+[[Category: Shveta B]]
-[[Category: Fold type ii plp-dependent enzyme]]
-[[Category: Lyase]]
-[[Category: Plp dependent enzyme]]
-[[Category: Tryptophan synthase beta subunit like family]]