2gw2: Difference between revisions

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==Crystal structure of the peptidyl-prolyl isomerase domain of human cyclophilin G==
==Crystal structure of the peptidyl-prolyl isomerase domain of human cyclophilin G==
<StructureSection load='2gw2' size='340' side='right' caption='[[2gw2]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
<StructureSection load='2gw2' size='340' side='right' caption='[[2gw2]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PPIG ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PPIG ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=2gw2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2gw2 OCA], [http://pdbe.org/2gw2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2gw2 RCSB], [http://www.ebi.ac.uk/pdbsum/2gw2 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=2gw2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2gw2 OCA], [http://pdbe.org/2gw2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2gw2 RCSB], [http://www.ebi.ac.uk/pdbsum/2gw2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2gw2 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2gw2 ConSurf].
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2gw2 ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
==See Also==
*[[Cyclophilin|Cyclophilin]]
__TOC__
__TOC__
</StructureSection>
</StructureSection>

Revision as of 11:01, 18 October 2017

Crystal structure of the peptidyl-prolyl isomerase domain of human cyclophilin GCrystal structure of the peptidyl-prolyl isomerase domain of human cyclophilin G

Structural highlights

2gw2 is a 1 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Gene:PPIG (HUMAN)
Activity:Peptidylprolyl isomerase, with EC number 5.2.1.8
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[PPIG_HUMAN] PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. May be implicated in the folding, transport, and assembly of proteins. May play an important role in the regulation of pre-mRNA splicing.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

2gw2, resolution 1.80Å

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