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TitleConformational lability of lipases observed in the absence of an oil-water interface: crystallographic studies of enzymes from the fungi Humicola lanuginosa and Rhizopus delemar.
Journal, issue, pagesJ. Lipid Res., Vol. 35, Page 524-534, Year 1994
Publish dateDec 6, 1993 (structure data deposition date)
AuthorsDerewenda, U. / Swenson, L. / Wei, Y. / Green, R. / Kobos, P.M. / Joerger, R. / Haas, M.J. / Derewenda, Z.S.
External linksPubMed:8014587
MethodsX-ray diffraction
Resolution1.84 - 2.6 Å
Structure data

PDB-1tib:
CONFORMATIONAL LABILITY OF LIPASES OBSERVED IN THE ABSENCE OF AN OIL-WATER INTERFACE: CRYSTALLOGRAPHIC STUDIES OF ENZYMES FROM THE FUNGI HUMICOLA LANUGINOSA AND RHIZOPUS DELEMAR
Method: X-RAY DIFFRACTION / Resolution: 1.84 Å

PDB-1tic:
CONFORMATIONAL LABILITY OF LIPASES OBSERVED IN THE ABSENCE OF AN OIL-WATER INTERFACE: CRYSTALLOGRAPHIC STUDIES OF ENZYMES FROM THE FUNGI HUMICOLA LANUGINOSA AND RHIZOPUS DELEMAR
Method: X-RAY DIFFRACTION / Resolution: 2.6 Å

Chemicals

ChemComp-HOH:
WATER

Source
  • thermomyces lanuginosus (fungus)
  • rhizopus oryzae (fungus)
KeywordsHYDROLASE(CARBOXYLIC ESTERASE) / HYDROLASE

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