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4n1q

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==Structure of Cyclophilin A in complex with cyclohexanecarboxamide.==
==Structure of Cyclophilin A in complex with cyclohexanecarboxamide.==
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<StructureSection load='4n1q' size='340' side='right' caption='[[4n1q]], [[Resolution|resolution]] 1.65&Aring;' scene=''>
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<StructureSection load='4n1q' size='340' side='right'caption='[[4n1q]], [[Resolution|resolution]] 1.65&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4n1q]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4N1Q OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4N1Q FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4n1q]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4N1Q OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4N1Q FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=WM2:CYCLOHEXANECARBOXAMIDE'>WM2</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]] 1.65&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4n1m|4n1m]], [[4n1n|4n1n]], [[4n1o|4n1o]], [[4n1p|4n1p]], [[4n1r|4n1r]], [[4n1s|4n1s]]</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=WM2:CYCLOHEXANECARBOXAMIDE'>WM2</scene></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'>[https://proteopedia.org/fgij/fg.htm?mol=4n1q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4n1q OCA], [https://pdbe.org/4n1q PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4n1q RCSB], [https://www.ebi.ac.uk/pdbsum/4n1q PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4n1q ProSAT]</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=4n1q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4n1q OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4n1q RCSB], [http://www.ebi.ac.uk/pdbsum/4n1q PDBsum]</span></td></tr>
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</table>
</table>
== Function ==
== Function ==
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[[http://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.
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==See Also==
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*[[Cyclophilin 3D structures|Cyclophilin 3D structures]]
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Peptidylprolyl isomerase]]
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[[Category: Homo sapiens]]
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[[Category: Dornan, J]]
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[[Category: Large Structures]]
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[[Category: Mcnae, I W]]
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[[Category: Dornan J]]
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[[Category: Walkinshaw, M D]]
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[[Category: Mcnae IW]]
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[[Category: Beta barrel]]
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[[Category: Walkinshaw MD]]
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[[Category: Cytosolic]]
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[[Category: Isomerase]]
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[[Category: Ligand complex]]
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[[Category: Prolyl cis/trans isomerase]]
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Current revision

Structure of Cyclophilin A in complex with cyclohexanecarboxamide.

PDB ID 4n1q

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