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==Structure of Cyclophilin B from Brugia malayi== | ==Structure of Cyclophilin B from Brugia malayi== | ||
<StructureSection load='4jcp' size='340' side='right' caption='[[4jcp]], [[Resolution|resolution]] 1.65Å' scene=''> | <StructureSection load='4jcp' size='340' side='right' caption='[[4jcp]], [[Resolution|resolution]] 1.65Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4jcp]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[4jcp]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Bruma Bruma]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4JCP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4JCP FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</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=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Bm1_55850 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=6279 | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Bm1_55850 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=6279 BRUMA])</td></tr> | ||
<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> | <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> | ||
<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=4jcp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4jcp OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4jcp RCSB], [http://www.ebi.ac.uk/pdbsum/4jcp PDBsum]</span></td></tr> | <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=4jcp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4jcp OCA], [http://pdbe.org/4jcp PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4jcp RCSB], [http://www.ebi.ac.uk/pdbsum/4jcp PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4jcp ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[[http://www.uniprot.org/uniprot/A8QGU4_BRUMA A8QGU4_BRUMA]] 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] | [[http://www.uniprot.org/uniprot/A8QGU4_BRUMA A8QGU4_BRUMA]] 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] | ||
==See Also== | |||
*[[Cyclophilin|Cyclophilin]] | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Bruma]] | ||
[[Category: Peptidylprolyl isomerase]] | [[Category: Peptidylprolyl isomerase]] | ||
[[Category: Structural genomic]] | [[Category: Structural genomic]] | ||
Revision as of 17:49, 5 August 2016
Structure of Cyclophilin B from Brugia malayiStructure of Cyclophilin B from Brugia malayi
Structural highlights
Function[A8QGU4_BRUMA] 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] See Also |
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