4nnr: Difference between revisions

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 ==FKBP13-FK506 Complex==
-<StructureSection load='4nnr' size='340' side='right' caption='[[4nnr]], [[Resolution|resolution]] 1.98&Aring;' scene=''>
+<StructureSection load='4nnr' size='340' side='right'caption='[[4nnr]], [[Resolution|resolution]] 1.98&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[4nnr]] 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=4NNR OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4NNR FirstGlance]. <br>
+<table><tr><td colspan='2'>[[4nnr]] is a 2 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=4NNR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4NNR FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FK5:8-DEETHYL-8-[BUT-3-ENYL]-ASCOMYCIN'>FK5</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]] 1.98&#8491;</td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">FKBP2, FKBP13 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FK5:8-DEETHYL-8-[BUT-3-ENYL]-ASCOMYCIN'>FK5</scene></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'>[https://proteopedia.org/fgij/fg.htm?mol=4nnr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4nnr OCA], [https://pdbe.org/4nnr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4nnr RCSB], [https://www.ebi.ac.uk/pdbsum/4nnr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4nnr ProSAT]</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=4nnr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4nnr OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4nnr RCSB], [http://www.ebi.ac.uk/pdbsum/4nnr PDBsum]</span></td></tr>
 </table>
+== Function ==
+[https://www.uniprot.org/uniprot/FKBP2_HUMAN FKBP2_HUMAN] PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.
 ==See Also==
-*[[FK506 binding protein|FK506 binding protein]]
+*[[FKBP 3D structures|FKBP 3D structures]]
 __TOC__
 </StructureSection>
-[[Category: Human]]
+[[Category: Homo sapiens]]
-[[Category: Peptidylprolyl isomerase]]
+[[Category: Large Structures]]
-[[Category: Clardy, J]]
+[[Category: Clardy J]]
-[[Category: Liang, J]]
+[[Category: Liang J]]
-[[Category: Martin, P K]]
+[[Category: Martin PK]]
-[[Category: Schreiber, S L]]
+[[Category: Schreiber SL]]
-[[Category: Schultz, L W]]
+[[Category: Schultz LW]]
-[[Category: Fkbp]]
-[[Category: Immunophilin]]
-[[Category: Isomerase]]
-[[Category: Isomerase-isomerase inhibitor complex]]
-[[Category: Loop crossing]]
-[[Category: Peptidyl-prolyl isomerase]]