This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
4jcp
From Proteopedia
(Difference between revisions)
| Line 1: | Line 1: | ||
| + | |||
==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 14:49, 5 August 2016
Structure of Cyclophilin B from Brugia malayi
| |||||||||||
