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TitleSphingomonas sp. KT-1 PahZ2 Structure Reveals a Role for Conformational Dynamics in Peptide Bond Hydrolysis.
Journal, issue, pagesJ. Phys. Chem. B, Vol. 125, Page 5722-5739, Year 2021
Publish dateJan 29, 2021 (structure data deposition date)
AuthorsBrambley, C.A. / Yared, T.J. / Gonzalez, M. / Jansch, A.L. / Wallen, J.R. / Weiland, M.H. / Miller, J.M.
External linksJ. Phys. Chem. B / PubMed:34060838
MethodsX-ray diffraction
Resolution1.85 - 2.5 Å
Structure data

PDB-7ljh:
Structure of poly(aspartic acid) hydrolase PahZ2 with Zn+2 bound
Method: X-RAY DIFFRACTION / Resolution: 2.5 Å

PDB-7lji:
Structure of poly(aspartic acid) hydrolase PahZ2 with Gd+3 bound
Method: X-RAY DIFFRACTION / Resolution: 1.85 Å

Chemicals

ChemComp-ZN:
Unknown entry

ChemComp-HOH:
WATER

ChemComp-GD3:
GADOLINIUM ION

Source
  • sphingomonas sp. kt-1 (bacteria)
KeywordsHYDROLASE / serine protease / poly(aspartic acid) hydrolase

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