4n1m: Difference between revisions

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<StructureSection load='4n1m' size='340' side='right'caption='[[4n1m]], [[Resolution|resolution]] 1.15&Aring;' scene=''>
<StructureSection load='4n1m' size='340' side='right'caption='[[4n1m]], [[Resolution|resolution]] 1.15&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4n1m]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4N1M OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4N1M FirstGlance]. <br>
<table><tr><td colspan='2'>[[4n1m]] 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=4N1M OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4N1M FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GLY:GLYCINE'>GLY</scene>, <scene name='pdbligand=PRO:PROLINE'>PRO</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.15&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4n1n|4n1n]], [[4n1o|4n1o]], [[4n1p|4n1p]], [[4n1q|4n1q]], [[4n1r|4n1r]], [[4n1s|4n1s]]</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GLY:GLYCINE'>GLY</scene>, <scene name='pdbligand=PRO:PROLINE'>PRO</scene></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PPIA, CYPA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4n1m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4n1m OCA], [https://pdbe.org/4n1m PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4n1m RCSB], [https://www.ebi.ac.uk/pdbsum/4n1m PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4n1m ProSAT]</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=4n1m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4n1m OCA], [http://pdbe.org/4n1m PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4n1m RCSB], [http://www.ebi.ac.uk/pdbsum/4n1m PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4n1m ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[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.  
[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.


==See Also==
==See Also==
*[[Cyclophilin|Cyclophilin]]
*[[Cyclophilin 3D structures|Cyclophilin 3D structures]]
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Human]]
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Peptidylprolyl isomerase]]
[[Category: Mcnae IW]]
[[Category: Mcnae, I W]]
[[Category: Patterson A]]
[[Category: Patterson, A]]
[[Category: Walkinshaw MD]]
[[Category: Walkinshaw, M D]]
[[Category: Beta barrel]]
[[Category: Cytosolic]]
[[Category: Isomerase]]
[[Category: Ligand complex]]
[[Category: Prolyl cis/trans isomerase]]

Latest revision as of 15:30, 1 March 2024

Structure of Cyclophilin A in complex with GlyPro.Structure of Cyclophilin A in complex with GlyPro.

Structural highlights

4n1m is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.15Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

PPIA_HUMAN PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.

See Also

4n1m, resolution 1.15Å

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