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6wdu
From Proteopedia
(Difference between revisions)
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| - | ==== | + | ==The external aldimine form of the Salmonella thypi wild-type tryptophan synthase in open conformation showing multiple side chain conformations for the residue beta Q114 and sodium ion at the metal coordination site. One of the beta-Q114 rotamer conformations allows a hydrogen bond to form with the PLP oxygen at the position 3 in the ring.== |
| - | <StructureSection load='6wdu' size='340' side='right'caption='[[6wdu]]' scene=''> | + | <StructureSection load='6wdu' size='340' side='right'caption='[[6wdu]], [[Resolution|resolution]] 1.40Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id= OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol= FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6wdu]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Salmonella_enterica_subsp._enterica_serovar_Typhimurium_str._LT2 Salmonella enterica subsp. enterica serovar Typhimurium str. LT2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6WDU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6WDU FirstGlance]. <br> |
| - | </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=6wdu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6wdu OCA], [https://pdbe.org/6wdu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6wdu RCSB], [https://www.ebi.ac.uk/pdbsum/6wdu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6wdu ProSAT]</span></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]] 1.4Å</td></tr> |
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DMS:DIMETHYL+SULFOXIDE'>DMS</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=KOU:(E)-N-({3-HYDROXY-2-METHYL-5-[(PHOSPHONOOXY)METHYL]PYRIDIN-4-YL}METHYLIDENE)-L-SERINE'>KOU</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</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=6wdu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6wdu OCA], [https://pdbe.org/6wdu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6wdu RCSB], [https://www.ebi.ac.uk/pdbsum/6wdu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6wdu ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/TRPB_SALTY TRPB_SALTY] The beta subunit is responsible for the synthesis of L-tryptophan from indole and L-serine. | ||
| + | |||
| + | ==See Also== | ||
| + | *[[Tryptophan synthase 3D structures|Tryptophan synthase 3D structures]] | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: | + | [[Category: Salmonella enterica subsp. enterica serovar Typhimurium str. LT2]] |
| + | [[Category: Dunn MF]] | ||
| + | [[Category: Fan L]] | ||
| + | [[Category: Hilario E]] | ||
| + | [[Category: Mueller LJ]] | ||
Current revision
The external aldimine form of the Salmonella thypi wild-type tryptophan synthase in open conformation showing multiple side chain conformations for the residue beta Q114 and sodium ion at the metal coordination site. One of the beta-Q114 rotamer conformations allows a hydrogen bond to form with the PLP oxygen at the position 3 in the ring.
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