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| | <StructureSection load='4d3s' size='340' side='right'caption='[[4d3s]], [[Resolution|resolution]] 2.24Å' scene=''> | | <StructureSection load='4d3s' size='340' side='right'caption='[[4d3s]], [[Resolution|resolution]] 2.24Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4d3s]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Ccim_a.s.4.1195 Ccim a.s.4.1195]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4D3S OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4D3S FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4d3s]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Nocardiopsis_halophila Nocardiopsis halophila]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4D3S OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4D3S FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BOG:B-OCTYLGLUCOSIDE'>BOG</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BOG:B-OCTYLGLUCOSIDE'>BOG</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4d3d|4d3d]], [[4d3f|4d3f]]</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=4d3s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4d3s OCA], [https://pdbe.org/4d3s PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4d3s RCSB], [https://www.ebi.ac.uk/pdbsum/4d3s PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4d3s 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/Dihydrofolate_reductase Dihydrofolate reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.5.1.3 1.5.1.3] </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=4d3s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4d3s OCA], [http://pdbe.org/4d3s PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4d3s RCSB], [http://www.ebi.ac.uk/pdbsum/4d3s PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4d3s ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [[https://www.uniprot.org/uniprot/A0A0J9X1X6_9ACTN A0A0J9X1X6_9ACTN]] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Ccim a s.4 1195]] | |
| - | [[Category: Dihydrofolate reductase]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Grogan, G]] | + | [[Category: Nocardiopsis halophila]] |
| - | [[Category: Hart, S]] | + | [[Category: Grogan G]] |
| - | [[Category: Man, H]] | + | [[Category: Hart S]] |
| - | [[Category: Turkenburg, J P]] | + | [[Category: Man H]] |
| - | [[Category: Nadph]]
| + | [[Category: Turkenburg JP]] |
| - | [[Category: Oxidoreductase]]
| + | |
| Structural highlights
Function
[A0A0J9X1X6_9ACTN]
Publication Abstract from PubMed
Oxidoreductases from Streptomyces sp. GF3546 [3546-IRED], Bacillus cereus BAG3X2 (BcIRED) and Nocardiopsis halophila (NhIRED) each reduce prochiral 2-methylpyrroline (2MPN) to (S)-2-methylpyrrolidine with >95 % ee and also a number of other imine substrates with good selectivity. Structures of BcIRED and NhIRED have helped to identify conserved active site residues within this subgroup of imine reductases that have S selectivity towards 2MPN, including a tyrosine residue that has a possible role in catalysis and superimposes with an aspartate in related enzymes that display R selectivity towards the same substrate. Mutation of this tyrosine residue-Tyr169-in 3546-IRED to Phe resulted in a mutant of negligible activity. The data together provide structural evidence for the location and significance of the Tyr residue in this group of imine reductases, and permit a comparison of the active sites of enzymes that reduce 2MPN with either R or S selectivity.
Structure, Activity and Stereoselectivity of NADPH-Dependent Oxidoreductases Catalysing the S-Selective Reduction of the Imine Substrate 2-Methylpyrroline.,Man H, Wells E, Hussain S, Leipold F, Hart S, Turkenburg JP, Turner NJ, Grogan G Chembiochem. 2015 Mar 24. doi: 10.1002/cbic.201402625. PMID:25809902[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Man H, Wells E, Hussain S, Leipold F, Hart S, Turkenburg JP, Turner NJ, Grogan G. Structure, Activity and Stereoselectivity of NADPH-Dependent Oxidoreductases Catalysing the S-Selective Reduction of the Imine Substrate 2-Methylpyrroline. Chembiochem. 2015 Mar 24. doi: 10.1002/cbic.201402625. PMID:25809902 doi:http://dx.doi.org/10.1002/cbic.201402625
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