3bt8

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<StructureSection load='3bt8' size='340' side='right'caption='[[3bt8]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
<StructureSection load='3bt8' size='340' side='right'caption='[[3bt8]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3bt8]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Leido Leido]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3BT8 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=3BT8 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3bt8]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Leido Leido]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3BT8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3BT8 FirstGlance]. <br>
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</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2haq|2haq]]</td></tr>
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</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2haq|2haq]]</div></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='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'>[http://proteopedia.org/fgij/fg.htm?mol=3bt8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3bt8 OCA], [http://pdbe.org/3bt8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3bt8 RCSB], [http://www.ebi.ac.uk/pdbsum/3bt8 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3bt8 ProSAT]</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=3bt8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3bt8 OCA], [https://pdbe.org/3bt8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3bt8 RCSB], [https://www.ebi.ac.uk/pdbsum/3bt8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3bt8 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/Q9U9R3_LEIDO Q9U9R3_LEIDO]] PPIases accelerate the folding of proteins.[RuleBase:RU000493] PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.[RuleBase:RU004223]
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[[https://www.uniprot.org/uniprot/Q9U9R3_LEIDO Q9U9R3_LEIDO]] PPIases accelerate the folding of proteins.[RuleBase:RU000493] PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.[RuleBase:RU004223]
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]

Revision as of 07:28, 10 November 2021

Crystal Structure of Mutant Cyclophilin (R147A) from Leishmania donovani

PDB ID 3bt8

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