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1jns

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==NMR Structure of the E. coli Peptidyl-Prolyl cis/trans-Isomerase Parvulin 10==
==NMR Structure of the E. coli Peptidyl-Prolyl cis/trans-Isomerase Parvulin 10==
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<StructureSection load='1jns' size='340' side='right' caption='[[1jns]], [[NMR_Ensembles_of_Models | 18 NMR models]]' scene=''>
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<StructureSection load='1jns' size='340' side='right'caption='[[1jns]]' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[1jns]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JNS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1JNS FirstGlance]. <br>
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<table><tr><td colspan='2'>[[1jns]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JNS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1JNS FirstGlance]. <br>
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</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1jnt|1jnt]]</td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">parA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895])</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1jns FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jns OCA], [https://pdbe.org/1jns PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1jns RCSB], [https://www.ebi.ac.uk/pdbsum/1jns PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1jns ProSAT]</span></td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Peptidylprolyl_isomerase Peptidylprolyl isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.2.1.8 5.2.1.8] </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=1jns FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jns OCA], [http://pdbe.org/1jns PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1jns RCSB], [http://www.ebi.ac.uk/pdbsum/1jns PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1jns ProSAT]</span></td></tr>
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</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/PPIC_ECOLI PPIC_ECOLI]] PPIases accelerate the folding of proteins. It prefers amino acid residues with hydrophobic side chains like leucine and phenylalanine in the P1 position of the peptides substrates.
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[https://www.uniprot.org/uniprot/PPIC_ECOLI PPIC_ECOLI] PPIases accelerate the folding of proteins. It prefers amino acid residues with hydrophobic side chains like leucine and phenylalanine in the P1 position of the peptides substrates.
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
Check<jmol>
<jmolCheckbox>
<jmolCheckbox>
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<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/jn/1jns_consurf.spt"</scriptWhenChecked>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/jn/1jns_consurf.spt"</scriptWhenChecked>
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
<text>to colour the structure by Evolutionary Conservation</text>
<text>to colour the structure by Evolutionary Conservation</text>
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==See Also==
==See Also==
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*[[Cyclophilin|Cyclophilin]]
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*[[Cyclophilin 3D structures|Cyclophilin 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Bacillus coli migula 1895]]
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[[Category: Escherichia coli]]
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[[Category: Peptidylprolyl isomerase]]
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[[Category: Large Structures]]
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[[Category: Fischer, G]]
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[[Category: Fischer G]]
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[[Category: Gemmecker, G]]
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[[Category: Gemmecker G]]
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[[Category: Kessler, H]]
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[[Category: Kessler H]]
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[[Category: Kuehlewein, A]]
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[[Category: Kuehlewein A]]
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[[Category: Rahfeld, J U]]
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[[Category: Rahfeld JU]]
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[[Category: Schelbert, B]]
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[[Category: Schelbert B]]
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[[Category: Voll, G]]
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[[Category: Voll G]]
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[[Category: Alpha-beta sandwich]]
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[[Category: Cis peptide bond]]
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[[Category: Isomerase]]
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Current revision

NMR Structure of the E. coli Peptidyl-Prolyl cis/trans-Isomerase Parvulin 10

PDB ID 1jns

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