6e4e: Difference between revisions

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<StructureSection load='6e4e' size='340' side='right'caption='[[6e4e]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
<StructureSection load='6e4e' size='340' side='right'caption='[[6e4e]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[6e4e]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6E4E OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6E4E FirstGlance]. <br>
<table><tr><td colspan='2'>[[6e4e]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6E4E OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6E4E FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MMV:3-(2-{3-[(2,4-DIAMINO-6-ETHYLPYRIMIDIN-5-YL)OXY]PROPOXY}PHENYL)PROPANOIC+ACID'>MMV</scene>, <scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</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]] 1.9&#8491;</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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MMV:3-(2-{3-[(2,4-DIAMINO-6-ETHYLPYRIMIDIN-5-YL)OXY]PROPOXY}PHENYL)PROPANOIC+ACID'>MMV</scene>, <scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6e4e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6e4e OCA], [http://pdbe.org/6e4e PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6e4e RCSB], [http://www.ebi.ac.uk/pdbsum/6e4e PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6e4e ProSAT]</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=6e4e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6e4e OCA], [https://pdbe.org/6e4e PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6e4e RCSB], [https://www.ebi.ac.uk/pdbsum/6e4e PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6e4e ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/DYR_STAAU DYR_STAAU]] Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis.  
[https://www.uniprot.org/uniprot/DYR_STAAU DYR_STAAU] Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis.


==See Also==
==See Also==
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Dihydrofolate reductase]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Structural genomic]]
[[Category: Staphylococcus aureus]]
[[Category: Dhfr]]
[[Category: Folate]]
[[Category: Folic acid]]
[[Category: Inhibitor]]
[[Category: Malaria]]
[[Category: Mmv]]
[[Category: Niaid]]
[[Category: Oxidoreductase]]
[[Category: Oxidoreductase-inhibitor complex]]
[[Category: Ssgcid]]

Latest revision as of 06:18, 11 October 2023

Crystal structure of dihydrofolate reductase from Staphylococcus aureus MW2 bound to NADP and p218

6e4e, resolution 1.90Å

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