2h0g: Difference between revisions

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 ==Crystal Structure of DsbG T200M mutant==
-<StructureSection load='2h0g' size='340' side='right' caption='[[2h0g]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
+<StructureSection load='2h0g' size='340' side='right'caption='[[2h0g]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2h0g]] is a 2 chain structure with sequence from [http://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=2H0G OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2H0G FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2h0g]] 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=2H0G OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2H0G 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">[[1v58|1v58]], [[1v57|1v57]], [[2h0h|2h0h]], [[2h0i|2h0i]]</td></tr>
+<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1v58|1v58]], [[1v57|1v57]], [[2h0h|2h0h]], [[2h0i|2h0i]]</div></td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">dsbG ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895])</td></tr>
+<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">dsbG ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895])</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=2h0g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2h0g OCA], [http://pdbe.org/2h0g PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2h0g RCSB], [http://www.ebi.ac.uk/pdbsum/2h0g PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2h0g 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=2h0g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2h0g OCA], [https://pdbe.org/2h0g PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2h0g RCSB], [https://www.ebi.ac.uk/pdbsum/2h0g PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2h0g ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/DSBG_ECOLI DSBG_ECOLI]] Involved in disulfide bond formation. DsbG and DsbC are part of a periplasmic reducing system that controls the level of cysteine sulfenylation, and provides reducing equivalents to rescue oxidatively damaged secreted proteins such as ErfK, YbiS and YnhG. Probably also functions as a disulfide isomerase with a narrower substrate specificity than DsbC. DsbG is maintained in a reduced state by DsbD. Displays chaperone activity in both redox states in vitro.<ref>PMID:19965429</ref>
+[[https://www.uniprot.org/uniprot/DSBG_ECOLI DSBG_ECOLI]] Involved in disulfide bond formation. DsbG and DsbC are part of a periplasmic reducing system that controls the level of cysteine sulfenylation, and provides reducing equivalents to rescue oxidatively damaged secreted proteins such as ErfK, YbiS and YnhG. Probably also functions as a disulfide isomerase with a narrower substrate specificity than DsbC. DsbG is maintained in a reduced state by DsbD. Displays chaperone activity in both redox states in vitro.<ref>PMID:19965429</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 32: / Line 32: @@
 ==See Also==
-*[[Thiol:disulfide interchange protein|Thiol:disulfide interchange protein]]
+*[[Thiol:disulfide interchange protein 3D structures|Thiol:disulfide interchange protein 3D structures]]
 == References ==
 <references/>
@@ Line 38: / Line 38: @@
 </StructureSection>
 [[Category: Bacillus coli migula 1895]]
+[[Category: Large Structures]]
 [[Category: Bardwell, J C.A]]
 [[Category: Heras, B]]