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TitleThe 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.
Journal, issue, pagesTo be Published
Publish dateApr 1, 2020 (structure data deposition date)
AuthorsHilario, E. / Fan, L. / Dunn, M.F. / Mueller, L.J.
External linksSearch PubMed
MethodsX-ray diffraction
Resolution1.4 Å
Structure data

PDB-6wdu:
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.
Method: X-RAY DIFFRACTION / Resolution: 1.4 Å

Chemicals

ChemComp-EDO:
1,2-ETHANEDIOL

ChemComp-DMS:
DIMETHYL SULFOXIDE / DMSO, precipitant*YM

ChemComp-PEG:
DI(HYDROXYETHYL)ETHER

ChemComp-NA:
Unknown entry

ChemComp-KOU:
(E)-N-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methylidene)-L-serine

ChemComp-HOH:
WATER

Source
  • salmonella typhimurium (strain lt2 / sgsc1412 / atcc 700720) (bacteria)
KeywordsLYASE/LYASE INHIBITOR / lyase-inhibitor / protein complex / LYASE / LYASE-LYASE INHIBITOR complex

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