2xgy

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Current revision (10:26, 9 May 2024) (edit) (undo)
 
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<StructureSection load='2xgy' size='340' side='right'caption='[[2xgy]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
<StructureSection load='2xgy' size='340' side='right'caption='[[2xgy]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[2xgy]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/European_rabbit European rabbit] and [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2XGY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2XGY FirstGlance]. <br>
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<table><tr><td colspan='2'>[[2xgy]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2XGY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2XGY FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></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">X-ray diffraction, [[Resolution|Resolution]] 1.8&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1vbs|1vbs]], [[1oca|1oca]], [[1mf8|1mf8]], [[2cyh|2cyh]], [[1cwb|1cwb]], [[1vbt|1vbt]], [[1cwl|1cwl]], [[1m9e|1m9e]], [[1cwc|1cwc]], [[1cwo|1cwo]], [[1cwi|1cwi]], [[2x2c|2x2c]], [[1rmh|1rmh]], [[1cwj|1cwj]], [[2rmb|2rmb]], [[1m9c|1m9c]], [[1cwa|1cwa]], [[1cwf|1cwf]], [[3cyh|3cyh]], [[1m9y|1m9y]], [[4cyh|4cyh]], [[1m9f|1m9f]], [[1cwh|1cwh]], [[1bck|1bck]], [[1w8v|1w8v]], [[1awr|1awr]], [[1nmk|1nmk]], [[1mik|1mik]], [[1awv|1awv]], [[1m9d|1m9d]], [[1awt|1awt]], [[2cpl|2cpl]], [[1fgl|1fgl]], [[2x2a|2x2a]], [[1m9x|1m9x]], [[1cwk|1cwk]], [[1m63|1m63]], [[5cyh|5cyh]], [[2x2d|2x2d]], [[1ak4|1ak4]], [[1aws|1aws]], [[2alf|2alf]], [[3cys|3cys]], [[1w8l|1w8l]], [[2x25|2x25]], [[1w8m|1w8m]], [[1awu|1awu]], [[2rma|2rma]], [[1cwm|1cwm]], [[1awq|1awq]], [[2xgu|2xgu]]</div></td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Peptidylprolyl_isomerase Peptidylprolyl isomerase], with EC number [https://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'>[https://proteopedia.org/fgij/fg.htm?mol=2xgy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xgy OCA], [https://pdbe.org/2xgy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2xgy RCSB], [https://www.ebi.ac.uk/pdbsum/2xgy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2xgy 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=2xgy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xgy OCA], [https://pdbe.org/2xgy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2xgy RCSB], [https://www.ebi.ac.uk/pdbsum/2xgy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2xgy ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/PPIA_HUMAN PPIA_HUMAN]] PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.
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[https://www.uniprot.org/uniprot/PPIA_HUMAN PPIA_HUMAN] PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: European rabbit]]
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[[Category: Homo sapiens]]
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[[Category: Human]]
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[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Peptidylprolyl isomerase]]
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[[Category: Oryctolagus cuniculus]]
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[[Category: Goldstone, D C]]
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[[Category: Goldstone DC]]
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[[Category: Haire, L F]]
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[[Category: Haire LF]]
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[[Category: Robertson, L E]]
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[[Category: Robertson LE]]
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[[Category: Stoye, J P]]
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[[Category: Stoye JP]]
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[[Category: Taylor, I A]]
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[[Category: Taylor IA]]
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[[Category: Endogenous]]
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[[Category: Retroviral capsid]]
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[[Category: Viral protein-isomerase complex]]
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Current revision

Complex of Rabbit Endogenous Lentivirus (RELIK)Capsid with Cyclophilin A

PDB ID 2xgy

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