6nnc
From Proteopedia
(Difference between revisions)
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- | '''Unreleased structure''' | ||
- | + | ==Structure of Dihydrofolate reductase from Mycobacterium tuberculosis in complex with NADPH and pemetrexed== | |
- | + | <StructureSection load='6nnc' size='340' side='right'caption='[[6nnc]], [[Resolution|resolution]] 1.80Å' scene=''> | |
- | + | == Structural highlights == | |
- | + | <table><tr><td colspan='2'>[[6nnc]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6NNC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6NNC FirstGlance]. <br> | |
- | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CO:COBALT+(II)+ION'>CO</scene>, <scene name='pdbligand=LYA:2-{4-[2-(2-AMINO-4-OXO-4,7-DIHYDRO-3H-PYRROLO[2,3-D]PYRIMIDIN-5-YL)-ETHYL]-BENZOYLAMINO}-PENTANEDIOIC+ACID'>LYA</scene>, <scene name='pdbligand=NDP:NADPH+DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NDP</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | |
- | [[Category: | + | <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=6nnc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6nnc OCA], [http://pdbe.org/6nnc PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6nnc RCSB], [http://www.ebi.ac.uk/pdbsum/6nnc PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6nnc ProSAT]</span></td></tr> | ||
+ | </table> | ||
+ | == Function == | ||
+ | [[http://www.uniprot.org/uniprot/DYR_MYCTU DYR_MYCTU]] Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis. | ||
+ | __TOC__ | ||
+ | </StructureSection> | ||
+ | [[Category: Dihydrofolate reductase]] | ||
+ | [[Category: Large Structures]] | ||
+ | [[Category: Chavez-Pacheco, S M]] | ||
+ | [[Category: Dias, M V.B]] | ||
+ | [[Category: Ribeiro, J A]] | ||
+ | [[Category: Antifolate]] | ||
+ | [[Category: Biosynthetic protein]] |
Revision as of 10:46, 17 July 2019
Structure of Dihydrofolate reductase from Mycobacterium tuberculosis in complex with NADPH and pemetrexed
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