4nx6: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4nx6]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Ecoli Ecoli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4NX6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4NX6 FirstGlance]. <br> | <table><tr><td colspan='2'>[[4nx6]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Ecoli Ecoli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4NX6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4NX6 FirstGlance]. <br> | ||
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BME:BETA-MERCAPTOETHANOL'>BME</scene>, <scene name='pdbligand=FOL:FOLIC+ACID'>FOL</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</scene>< | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BME:BETA-MERCAPTOETHANOL'>BME</scene>, <scene name='pdbligand=FOL:FOLIC+ACID'>FOL</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</scene></td></tr> | ||
<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4kjk|4kjk]], [[4nx7|4nx7]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4kjk|4kjk]], [[4nx7|4nx7]]</td></tr> | ||
<tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">folA, tmrA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</td></tr> | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">folA, tmrA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</td></tr> | ||
<tr><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='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><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4nx6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4nx6 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4nx6 RCSB], [http://www.ebi.ac.uk/pdbsum/4nx6 PDBsum]</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=4nx6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4nx6 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4nx6 RCSB], [http://www.ebi.ac.uk/pdbsum/4nx6 PDBsum]</span></td></tr> | ||
<table> | </table> | ||
== Function == | |||
[[http://www.uniprot.org/uniprot/DYR_ECOLI DYR_ECOLI]] Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis. | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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Integrated description of protein dynamics from room-temperature X-ray crystallography and NMR.,Fenwick RB, van den Bedem H, Fraser JS, Wright PE Proc Natl Acad Sci U S A. 2014 Jan 28;111(4):E445-54. doi:, 10.1073/pnas.1323440111. Epub 2014 Jan 13. PMID:24474795<ref>PMID:24474795</ref> | Integrated description of protein dynamics from room-temperature X-ray crystallography and NMR.,Fenwick RB, van den Bedem H, Fraser JS, Wright PE Proc Natl Acad Sci U S A. 2014 Jan 28;111(4):E445-54. doi:, 10.1073/pnas.1323440111. Epub 2014 Jan 13. PMID:24474795<ref>PMID:24474795</ref> | ||
From | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
==See Also== | |||
*[[Dihydrofolate reductase|Dihydrofolate reductase]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
| Line 23: | Line 28: | ||
[[Category: Dihydrofolate reductase]] | [[Category: Dihydrofolate reductase]] | ||
[[Category: Ecoli]] | [[Category: Ecoli]] | ||
[[Category: Bedem, H van den | [[Category: Bedem, H van den]] | ||
[[Category: Fenwick, R B | [[Category: Fenwick, R B]] | ||
[[Category: Fraser, J S | [[Category: Fraser, J S]] | ||
[[Category: Wright, P E | [[Category: Wright, P E]] | ||
[[Category: Folate metabolism]] | [[Category: Folate metabolism]] | ||
[[Category: Oxidoreductase]] | [[Category: Oxidoreductase]] | ||
