3qcz
From Proteopedia
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| - | [[Image:3qcz.jpg|left|200px]] | ||
| - | < | + | ==Crystal structure of bifunctional folylpolyglutamate synthase/dihydrofolate synthase with Mn, AMPPNP and L-Glutamate bound== |
| - | + | <StructureSection load='3qcz' size='340' side='right'caption='[[3qcz]], [[Resolution|resolution]] 2.00Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[3qcz]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Yersinia_pestis_CO92 Yersinia pestis CO92]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3QCZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3QCZ FirstGlance]. <br> | |
| - | or | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2Å</td></tr> |
| - | -- | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ANP:PHOSPHOAMINOPHOSPHONIC+ACID-ADENYLATE+ESTER'>ANP</scene>, <scene name='pdbligand=GLU:GLUTAMIC+ACID'>GLU</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene></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=3qcz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qcz OCA], [https://pdbe.org/3qcz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3qcz RCSB], [https://www.ebi.ac.uk/pdbsum/3qcz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3qcz ProSAT]</span></td></tr> | |
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/A0A5P8YIK0_YERPE A0A5P8YIK0_YERPE] Functions in two distinct reactions of the de novo folate biosynthetic pathway. Catalyzes the addition of a glutamate residue to dihydropteroate (7,8-dihydropteroate or H2Pte) to form dihydrofolate (7,8-dihydrofolate monoglutamate or H2Pte-Glu). Also catalyzes successive additions of L-glutamate to tetrahydrofolate or 10-formyltetrahydrofolate or 5,10-methylenetetrahydrofolate, leading to folylpolyglutamate derivatives.[ARBA:ARBA00002714][PIRNR:PIRNR001563] | ||
| - | == | + | ==See Also== |
| - | + | *[[Folylpolyglutamate synthase|Folylpolyglutamate synthase]] | |
| - | + | __TOC__ | |
| - | + | </StructureSection> | |
| - | [[ | + | [[Category: Large Structures]] |
| - | [[Category: | + | [[Category: Yersinia pestis CO92]] |
| - | [[Category: Yersinia pestis]] | + | [[Category: Anderson W]] |
| - | [[Category: Anderson | + | [[Category: Joachimiak A]] |
| - | + | [[Category: Makowska-Grzyska M]] | |
| - | [[Category: Joachimiak | + | [[Category: Maltseva N]] |
| - | [[Category: | + | [[Category: Nocek B]] |
| - | [[Category: Maltseva | + | |
| - | [[Category: Nocek | + | |
Current revision
Crystal structure of bifunctional folylpolyglutamate synthase/dihydrofolate synthase with Mn, AMPPNP and L-Glutamate bound
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