4g2p

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==Crystal structure of peptidyl-prolyl cis-trans isomerase domain II of molecular chaperone SurA from Salmonella enterica subsp. enterica serovar Typhimurium str. 14028S==
==Crystal structure of peptidyl-prolyl cis-trans isomerase domain II of molecular chaperone SurA from Salmonella enterica subsp. enterica serovar Typhimurium str. 14028S==
<StructureSection load='4g2p' size='340' side='right' caption='[[4g2p]], [[Resolution|resolution]] 1.82&Aring;' scene=''>
<StructureSection load='4g2p' size='340' side='right' caption='[[4g2p]], [[Resolution|resolution]] 1.82&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4g2p]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Salmonella_enterica_subsp._enterica_serovar_typhimurium_str._14028s Salmonella enterica subsp. enterica serovar typhimurium str. 14028s]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4G2P OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4G2P FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4g2p]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Salt1 Salt1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4G2P OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4G2P FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</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"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">surA, STM14_0111 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=588858 Salmonella enterica subsp. enterica serovar Typhimurium str. 14028S])</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">surA, STM14_0111 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=588858 SALT1])</td></tr>
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<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=4g2p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4g2p OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4g2p RCSB], [http://www.ebi.ac.uk/pdbsum/4g2p PDBsum]</span></td></tr>
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<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=4g2p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4g2p OCA], [http://pdbe.org/4g2p PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4g2p RCSB], [http://www.ebi.ac.uk/pdbsum/4g2p PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4g2p ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Salmonella enterica subsp. enterica serovar typhimurium str. 14028s]]
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[[Category: Salt1]]
[[Category: Adkins, J N]]
[[Category: Adkins, J N]]
[[Category: Brown, R N]]
[[Category: Brown, R N]]

Revision as of 10:50, 5 August 2016

Crystal structure of peptidyl-prolyl cis-trans isomerase domain II of molecular chaperone SurA from Salmonella enterica subsp. enterica serovar Typhimurium str. 14028S

4g2p, resolution 1.82Å

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