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TitleStructure of formylglycine-generating enzyme in complex with copper and a substrate reveals an acidic pocket for binding and activation of molecular oxygen.
Journal, issue, pagesChem Sci, Vol. 10, Page 7049-7058, Year 2019
Publish dateJun 14, 2019 (structure data deposition date)
AuthorsMiarzlou, D.A. / Leisinger, F. / Joss, D. / Haussinger, D. / Seebeck, F.P.
External linksChem Sci / PubMed:31588272
MethodsX-ray diffraction
Resolution1.04 Å
Structure data

PDB-6s07:
Structure of formylglycine-generating enzyme at 1.04 A in complex with copper and substrate reveals an acidic pocket for binding and acti-vation of molecular oxygen.
Method: X-RAY DIFFRACTION / Resolution: 1.04 Å

Chemicals

ChemComp-CU1:
COPPER (I) ION

ChemComp-CA:
Unknown entry

ChemComp-CL:
Unknown entry

ChemComp-HOH:
WATER

Source
  • thermomonospora curvata (strain atcc 19995 / dsm 43183 / jcm 3096 / nbrc 15933 / ncimb 10081 / henssen b9) (bacteria)
  • thermomonospora curvata dsm 43183 (bacteria)
KeywordsTRANSFERASE / Formylglycine-generating enzyme / complex / substrate analog / copper

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