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Structure paper

TitleThe Structure of Allophanate Hydrolase from Granulibacter bethesdensis Provides Insights into Substrate Specificity in the Amidase Signature Family.
Journal, issue, pagesBiochemistry, Vol. 52, Page 690-700, Year 2013
Publish dateSep 5, 2012 (structure data deposition date)
AuthorsLin, Y. / St Maurice, M.
External linksBiochemistry / PubMed:23282241
MethodsX-ray diffraction
Resolution2.201 - 2.8 Å
Structure data

PDB-4gyr:
Granulibacter bethesdensis allophanate hydrolase apo
Method: X-RAY DIFFRACTION / Resolution: 2.8 Å

PDB-4gys:
Granulibacter bethesdensis allophanate hydrolase co-crystallized with malonate
Method: X-RAY DIFFRACTION / Resolution: 2.201 Å

Chemicals

ChemComp-HOH:
WATER

ChemComp-MLI:
MALONATE ION

Source
  • granulibacter bethesdensis (bacteria)
KeywordsHYDROLASE / Amidase signature family enzyme

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