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TitleThe Structure of Human DNase I Bound to Magnesium and Phosphate Ions Points to a Catalytic Mechanism Common to Members of the DNase I-Like Superfamily.
Journal, issue, pagesBiochemistry, Vol. 51, Page 10250-, Year 2012
Publish dateJun 4, 2012 (structure data deposition date)
AuthorsParsiegla, G. / Noguere, C. / Santell, L. / Lazarus, R.A. / Bourne, Y.
External linksBiochemistry / PubMed:23215638
MethodsX-ray diffraction
Resolution1.95 Å
Structure data

PDB-4awn:
Structure of recombinant human DNase I (rhDNaseI) in complex with Magnesium and Phosphate.
Method: X-RAY DIFFRACTION / Resolution: 1.95 Å

Chemicals

ChemComp-CA:
Unknown entry

ChemComp-MG:
Unknown entry

ChemComp-PO4:
PHOSPHATE ION

ChemComp-BTB:
2-[BIS-(2-HYDROXY-ETHYL)-AMINO]-2-HYDROXYMETHYL-PROPANE-1,3-DIOL / pH buffer*YM

ChemComp-NAG:
2-acetamido-2-deoxy-beta-D-glucopyranose

ChemComp-HOH:
WATER

Source
  • homo sapiens (human)
KeywordsHYDROLASE / ENDONUCLEASE / PULMOZYME

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