4hb7
From Proteopedia
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==The Structure of Dihydropteroate Synthase from Staphylococcus aureus subsp. aureus Mu50.== | ==The Structure of Dihydropteroate Synthase from Staphylococcus aureus subsp. aureus Mu50.== | ||
<StructureSection load='4hb7' size='340' side='right' caption='[[4hb7]], [[Resolution|resolution]] 1.95Å' scene=''> | <StructureSection load='4hb7' size='340' side='right' caption='[[4hb7]], [[Resolution|resolution]] 1.95Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[4hb7]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/ | + | <table><tr><td colspan='2'>[[4hb7]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Staam Staam]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4HB7 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4HB7 FirstGlance]. <br> |
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene></td></tr> | ||
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">folP, SAV0514 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=158878 | + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">folP, SAV0514 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=158878 STAAM])</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=4hb7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4hb7 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4hb7 RCSB], [http://www.ebi.ac.uk/pdbsum/4hb7 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=4hb7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4hb7 OCA], [http://pdbe.org/4hb7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4hb7 RCSB], [http://www.ebi.ac.uk/pdbsum/4hb7 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4hb7 ProSAT]</span></td></tr> |
</table> | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/DHPS_STAAM DHPS_STAAM]] DHPS catalyzes the formation of the immediate precursor of folic acid. It is implicated in resistance to sulfonamide. | ||
==See Also== | ==See Also== | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Dihydropteroate synthase]] | [[Category: Dihydropteroate synthase]] | ||
| - | [[Category: | + | [[Category: Staam]] |
[[Category: Baker, D]] | [[Category: Baker, D]] | ||
[[Category: Cuff, M E]] | [[Category: Cuff, M E]] | ||
Revision as of 08:09, 11 August 2016
The Structure of Dihydropteroate Synthase from Staphylococcus aureus subsp. aureus Mu50.
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Categories: Dihydropteroate synthase | Staam | Baker, D | Cuff, M E | Guinn, K | Holowicki, J | Ioerger, T R | Jedrzejczak, R | Joachimiak, A | Structural genomic | MTBI, Structures of Mtb Proteins Conferring Susceptibility to Known Mtb Inhibitors | Rubin, E J | Sacchettini, J C | Terwilliger, T C | Transferase
