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2fzj
From Proteopedia
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==New Insights into DHFR Interactions: Analysis of Pneumocystis carinii and Mouse DHFR Complexes with NADPH and Two Highly Potent Trimethoprim Derivatives== | ==New Insights into DHFR Interactions: Analysis of Pneumocystis carinii and Mouse DHFR Complexes with NADPH and Two Highly Potent Trimethoprim Derivatives== | ||
| - | <StructureSection load='2fzj' size='340' side='right' caption='[[2fzj]], [[Resolution|resolution]] 2.00Å' scene=''> | + | <StructureSection load='2fzj' size='340' side='right'caption='[[2fzj]], [[Resolution|resolution]] 2.00Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[2fzj]] is a 1 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[2fzj]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FZJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2FZJ FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=DH3:2,4-DIAMINO-5-[3,4-DIMETHOXY-5-(5-CARBOXYL-1-PENTYNYL)]BENZYL+PYRIMIDINE'>DH3</scene>, <scene name='pdbligand=NDP:NADPH+DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NDP</scene | + | </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=DH3:2,4-DIAMINO-5-[3,4-DIMETHOXY-5-(5-CARBOXYL-1-PENTYNYL)]BENZYL+PYRIMIDINE'>DH3</scene>, <scene name='pdbligand=NDP:NADPH+DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NDP</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=2fzj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fzj OCA], [https://pdbe.org/2fzj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2fzj RCSB], [https://www.ebi.ac.uk/pdbsum/2fzj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2fzj ProSAT]</span></td></tr> | |
| - | + | ||
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | |
</table> | </table> | ||
== Function == | == Function == | ||
| - | [ | + | [https://www.uniprot.org/uniprot/DYR_MOUSE DYR_MOUSE] Key enzyme in folate metabolism. Contributes to the de novo mitochondrial thymidylate biosynthesis pathway. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis. Binds its own mRNA and that of DHFRL1. |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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==See Also== | ==See Also== | ||
| - | *[[Dihydrofolate reductase|Dihydrofolate reductase]] | + | *[[Dihydrofolate reductase 3D structures|Dihydrofolate reductase 3D structures]] |
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Large Structures]] |
| - | [[Category: | + | [[Category: Mus musculus]] |
| - | [[Category: Chisum | + | [[Category: Chisum K]] |
| - | [[Category: Cody | + | [[Category: Cody V]] |
| - | [[Category: Pace | + | [[Category: Pace J]] |
| - | [[Category: Rosowsky | + | [[Category: Rosowsky A]] |
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Current revision
New Insights into DHFR Interactions: Analysis of Pneumocystis carinii and Mouse DHFR Complexes with NADPH and Two Highly Potent Trimethoprim Derivatives
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Categories: Large Structures | Mus musculus | Chisum K | Cody V | Pace J | Rosowsky A

