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==HUMAN CYCLOPHILIN A COMPLEXED WITH 4 MEILE CYCLOSPORIN==
==HUMAN CYCLOPHILIN A COMPLEXED WITH 4 MEILE CYCLOSPORIN==
<StructureSection load='1cwm' size='340' side='right' caption='[[1cwm]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
<StructureSection load='1cwm' size='340' side='right'caption='[[1cwm]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1cwm]] is a 2 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=1CWM OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1CWM FirstGlance]. <br>
<table><tr><td colspan='2'>[[1cwm]] is a 2 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=1CWM OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1CWM FirstGlance]. <br>
</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=ABA:ALPHA-AMINOBUTYRIC+ACID'>ABA</scene>, <scene name='pdbligand=BMT:4-METHYL-4-[(E)-2-BUTENYL]-4,N-METHYL-THREONINE'>BMT</scene>, <scene name='pdbligand=DAL:D-ALANINE'>DAL</scene>, <scene name='pdbligand=IML:N-METHYL-ISOLEUCINE'>IML</scene>, <scene name='pdbligand=MLE:N-METHYLLEUCINE'>MLE</scene>, <scene name='pdbligand=MVA:N-METHYLVALINE'>MVA</scene>, <scene name='pdbligand=SAR:SARCOSINE'>SAR</scene></td></tr>
</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=ABA:ALPHA-AMINOBUTYRIC+ACID'>ABA</scene>, <scene name='pdbligand=BMT:4-METHYL-4-[(E)-2-BUTENYL]-4,N-METHYL-THREONINE'>BMT</scene>, <scene name='pdbligand=DAL:D-ALANINE'>DAL</scene>, <scene name='pdbligand=IML:N-METHYL-ISOLEUCINE'>IML</scene>, <scene name='pdbligand=MLE:N-METHYLLEUCINE'>MLE</scene>, <scene name='pdbligand=MVA:N-METHYLVALINE'>MVA</scene>, <scene name='pdbligand=SAR:SARCOSINE'>SAR</scene></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1bck|1bck]], [[1c5f|1c5f]], [[1csa|1csa]], [[1cwa|1cwa]], [[1cwb|1cwb]], [[1cwc|1cwc]], [[1cwf|1cwf]], [[1cwh|1cwh]], [[1cwi|1cwi]], [[1cwj|1cwj]], [[1cwk|1cwk]], [[1cwl|1cwl]], [[1cwo|1cwo]], [[1cya|1cya]], [[1cyb|1cyb]], [[1cyn|1cyn]], [[1ikf|1ikf]], [[1m63|1m63]], [[1mf8|1mf8]], [[1mik|1mik]], [[1qng|1qng]], [[1qnh|1qnh]], [[1xq7|1xq7]], [[2esl|2esl]], [[2oju|2oju]], [[2poy|2poy]], [[2rma|2rma]], [[2rmb|2rmb]], [[2rmc|2rmc]], [[2wfj|2wfj]], [[2x2c|2x2c]], [[2x7k|2x7k]], [[2z6w|2z6w]], [[3bo7|3bo7]], [[3cys|3cys]], [[3eov|3eov]]</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1bck|1bck]], [[1c5f|1c5f]], [[1csa|1csa]], [[1cwa|1cwa]], [[1cwb|1cwb]], [[1cwc|1cwc]], [[1cwf|1cwf]], [[1cwh|1cwh]], [[1cwi|1cwi]], [[1cwj|1cwj]], [[1cwk|1cwk]], [[1cwl|1cwl]], [[1cwo|1cwo]], [[1cya|1cya]], [[1cyb|1cyb]], [[1cyn|1cyn]], [[1ikf|1ikf]], [[1m63|1m63]], [[1mf8|1mf8]], [[1mik|1mik]], [[1qng|1qng]], [[1qnh|1qnh]], [[1xq7|1xq7]], [[2esl|2esl]], [[2oju|2oju]], [[2poy|2poy]], [[2rma|2rma]], [[2rmb|2rmb]], [[2rmc|2rmc]], [[2wfj|2wfj]], [[2x2c|2x2c]], [[2x7k|2x7k]], [[2z6w|2z6w]], [[3bo7|3bo7]], [[3cys|3cys]], [[3eov|3eov]]</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CYCLOPHILIN ([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">CYCLOPHILIN ([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=1cwm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cwm OCA], [http://pdbe.org/1cwm PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1cwm RCSB], [http://www.ebi.ac.uk/pdbsum/1cwm PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1cwm ProSAT]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1cwm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cwm OCA], [http://pdbe.org/1cwm PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1cwm RCSB], [http://www.ebi.ac.uk/pdbsum/1cwm PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1cwm ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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==See Also==
==See Also==
*[[Cyclophilin|Cyclophilin]]
*[[Cyclophilin 3D structures|Cyclophilin 3D structures]]
== References ==
== References ==
<references/>
<references/>
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</StructureSection>
</StructureSection>
[[Category: Human]]
[[Category: Human]]
[[Category: Large Structures]]
[[Category: Peptidylprolyl isomerase]]
[[Category: Peptidylprolyl isomerase]]
[[Category: Kallen, J]]
[[Category: Kallen, J]]

Revision as of 13:19, 18 November 2020

HUMAN CYCLOPHILIN A COMPLEXED WITH 4 MEILE CYCLOSPORINHUMAN CYCLOPHILIN A COMPLEXED WITH 4 MEILE CYCLOSPORIN

Structural highlights

1cwm is a 2 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
NonStd Res:, , , , , ,
Gene:CYCLOPHILIN (HUMAN)
Activity:Peptidylprolyl isomerase, with EC number 5.2.1.8
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.

Evolutionary Conservation

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

Publication Abstract from PubMed

Eight new X-ray structures of different cyclophilin A/cyclosporin-derivative complexes are presented. These structures, combined with the existing three published cyclosporin complexes, provide a useful structural database for the analysis of protein-ligand interactions. The effect of small chemical differences on protein-ligand hydrogen-bonding, van der Waals interactions and water structure is presented.

X-ray structures and analysis of 11 cyclosporin derivatives complexed with cyclophilin A.,Kallen J, Mikol V, Taylor P, Walkinshaw MD J Mol Biol. 1998 Oct 23;283(2):435-49. PMID:9769216[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. ↑ Kallen J, Mikol V, Taylor P, Walkinshaw MD. X-ray structures and analysis of 11 cyclosporin derivatives complexed with cyclophilin A. J Mol Biol. 1998 Oct 23;283(2):435-49. PMID:9769216

1cwm, resolution 2.00Å

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