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TitleCrystal structure and enzymatic characterization of the putative adenylyl cyclase HpAC1 from Hippeastrum reveal dominant triphosphatase activity.
Journal, issue, pagesJ. Struct. Biol., Vol. 212, Page 107649-107649, Year 2020
Publish dateApr 15, 2020 (structure data deposition date)
AuthorsKleinboelting, S. / Miehling, J. / Steegborn, C.
External linksJ. Struct. Biol. / PubMed:33075486
MethodsX-ray diffraction
Resolution1.94541097376 Å
Structure data

PDB-6yp4:
Putative adenylyl cyclase HpAC1 from Hippeastrum reveals a dominant triphophatase activity
Method: X-RAY DIFFRACTION / Resolution: 1.94541097376 Å

Chemicals

ChemComp-GCP:
PHOSPHOMETHYLPHOSPHONIC ACID GUANYLATE ESTER / GMP-PCP, energy-carrying molecule analogue*YM

ChemComp-MG:
Unknown entry

ChemComp-CL:
Unknown entry

ChemComp-EDO:
1,2-ETHANEDIOL

ChemComp-HOH:
WATER

Source
  • hippeastrum hybrid cultivar (plant)
KeywordsHYDROLASE / Triphosphatase / plant / PPPase / GTP analog / substrate complex / substrate specificity

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