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Structure paper

TitleDiminishing returns and tradeoffs constrain the laboratory optimization of an enzyme
Journal, issue, pagesNat Commun, Vol. 3, Page 1257-1257, Year 2012
Publish dateMar 10, 2012 (structure data deposition date)
AuthorsTokuriki, N. / Jackson, C.J. / Afriat-Jurnou, L. / Wyganowski, K.T. / Tang, R. / Tawfik, D.S.
External linksNat Commun / PubMed:23212386
MethodsX-ray diffraction
Resolution1.5 - 1.85 Å
Structure data

PDB-4e3t:
Round 18 Arylesterase Variant of Phosphotriesterase with Bound Transition State Analog
Method: X-RAY DIFFRACTION / Resolution: 1.65 Å

PDB-4gy0:
Round 18 Arylesterase Variant of Phosphotriesterase
Method: X-RAY DIFFRACTION / Resolution: 1.85 Å

PDB-4gy1:
Round 18 Arylesterase Variant of Phosphotriesterase with Bound Cacodylate
Method: X-RAY DIFFRACTION / Resolution: 1.5 Å

Chemicals

ChemComp-ZN:
Unknown entry

ChemComp-HLN:
hexyl(naphthalen-2-yloxy)phosphinic acid

ChemComp-HOH:
WATER

ChemComp-CAC:
CACODYLATE ION

Source
  • brevundimonas diminuta (bacteria)
  • synthetic construct (others)
KeywordsHYDROLASE / phosphotriesterase / alpha/beta hydrolase / arylesterase / carboxylated lysine

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