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==The crystal structure of 7,8-dihydropteroate synthase from Vibrio fischeri ES114== | ==The crystal structure of 7,8-dihydropteroate synthase from Vibrio fischeri ES114== | ||
<StructureSection load='5usw' size='340' side='right' caption='[[5usw]], [[Resolution|resolution]] 1.64Å' scene=''> | <StructureSection load='5usw' size='340' side='right'caption='[[5usw]], [[Resolution|resolution]] 1.64Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5usw]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5USW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5USW FirstGlance]. <br> | <table><tr><td colspan='2'>[[5usw]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Alif1 Alif1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5USW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5USW FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=FMT:FORMIC+ACID'>FMT</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=FMT:FORMIC+ACID'>FMT</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr> | ||
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">folP, VF_0480 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=312309 ALIF1])</td></tr> | |||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Dihydropteroate_synthase Dihydropteroate synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.15 2.5.1.15] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Dihydropteroate_synthase Dihydropteroate synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.15 2.5.1.15] </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=5usw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5usw OCA], [http://pdbe.org/5usw PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5usw RCSB], [http://www.ebi.ac.uk/pdbsum/5usw PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5usw ProSAT]</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=5usw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5usw OCA], [http://pdbe.org/5usw PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5usw RCSB], [http://www.ebi.ac.uk/pdbsum/5usw PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5usw ProSAT]</span></td></tr> | ||
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== Function == | == Function == | ||
[[http://www.uniprot.org/uniprot/Q5E7M1_VIBF1 Q5E7M1_VIBF1]] Catalyzes the condensation of para-aminobenzoate (pABA) with 6-hydroxymethyl-7,8-dihydropterin diphosphate (DHPt-PP) to form 7,8-dihydropteroate (H2Pte), the immediate precursor of folate derivatives.[RuleBase:RU361205] | [[http://www.uniprot.org/uniprot/Q5E7M1_VIBF1 Q5E7M1_VIBF1]] Catalyzes the condensation of para-aminobenzoate (pABA) with 6-hydroxymethyl-7,8-dihydropterin diphosphate (DHPt-PP) to form 7,8-dihydropteroate (H2Pte), the immediate precursor of folate derivatives.[RuleBase:RU361205] | ||
==See Also== | |||
*[[Dihydropteroate synthase 3D structures|Dihydropteroate synthase 3D structures]] | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Alif1]] | |||
[[Category: Dihydropteroate synthase]] | [[Category: Dihydropteroate synthase]] | ||
[[Category: Large Structures]] | |||
[[Category: Anderson, W F]] | [[Category: Anderson, W F]] | ||
[[Category: Structural genomic]] | [[Category: Structural genomic]] | ||
Revision as of 11:00, 27 November 2019
The crystal structure of 7,8-dihydropteroate synthase from Vibrio fischeri ES114The crystal structure of 7,8-dihydropteroate synthase from Vibrio fischeri ES114
Structural highlights
Function[Q5E7M1_VIBF1] Catalyzes the condensation of para-aminobenzoate (pABA) with 6-hydroxymethyl-7,8-dihydropterin diphosphate (DHPt-PP) to form 7,8-dihydropteroate (H2Pte), the immediate precursor of folate derivatives.[RuleBase:RU361205] See Also |
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