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Structure paper

TitleCrystal Structure of Citrobacter Freundii Asp214Ala Tyrosine Phenol-Lyase Reveals that Asp214 is Critical for Maintaining a Strain in the Internal Aldimine
Journal, issue, pagesCroatica Chemica Acta, Vol. 85, Page 283-, Year 2012
Publish dateMay 3, 2011 (structure data deposition date)
AuthorsMilic, D. / Demidkina, T.V. / Zakomirdina, L.N. / Matkovic-Calogovic, D. / Antson, A.A.
External linksCroatica Chemica Acta / Search PubMed
MethodsX-ray diffraction
Resolution1.91 Å
Structure data

PDB-2yhk:
D214A mutant of tyrosine phenol-lyase from Citrobacter freundii
Method: X-RAY DIFFRACTION / Resolution: 1.91 Å

Chemicals

ChemComp-K:
Unknown entry

ChemComp-PG4:
TETRAETHYLENE GLYCOL / precipitant*YM

ChemComp-PEG:
DI(HYDROXYETHYL)ETHER

ChemComp-PLP:
PYRIDOXAL-5'-PHOSPHATE

ChemComp-P33:
3,6,9,12,15,18-HEXAOXAICOSANE-1,20-DIOL / precipitant*YM

ChemComp-HOH:
WATER

Source
  • citrobacter freundii (bacteria)
KeywordsLYASE / PYRIDOXAL-5'-PHOSPHATE-DEPENDENT ENZYME / BETA-ELIMINATION REACTION

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