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TitleGeneral features to enhance enzymatic activity of poly(ethylene terephthalate) hydrolysis.
Journal, issue, pagesNat Catal, Vol. 4, Page 425-430, Year 2021
Publish dateAug 30, 2020 (structure data deposition date)
AuthorsChe, C.C. / Han, X. / Li, X. / Jiang, P. / Niu, D. / Ma, L. / Liu, W. / Li, S. / Qu, Y. / Hu, H. ...Che, C.C. / Han, X. / Li, X. / Jiang, P. / Niu, D. / Ma, L. / Liu, W. / Li, S. / Qu, Y. / Hu, H. / Min, J. / Yang, Y. / Zhang, L. / Zeng, W. / Huang, J.W. / Dai, L. / Guo, R.T.
External linksNat Catal / Search PubMed
MethodsX-ray diffraction
Resolution1.32 - 1.65 Å
Structure data

PDB-7cwq:
Crystal structure of a novel cutinase from Burkhoderiales bacterium RIFCSPLOWO2_02_FULL_57_36
Method: X-RAY DIFFRACTION / Resolution: 1.65 Å

PDB-7cy0:
Crystal structure of S185H mutant PET hydrolase from Ideonella sakaiensis
Method: X-RAY DIFFRACTION / Resolution: 1.32 Å

Chemicals

ChemComp-SO4:
SULFATE ION

ChemComp-HOH:
WATER

ChemComp-ACY:
ACETIC ACID

Source
  • burkholderiales bacterium rifcsplowo2_02_full_57_36 (bacteria)
  • ideonella sakaiensis (strain nbrc 110686 / tistr 2288 / 201-f6) (bacteria)
KeywordsHYDROLASE / substrate binding / inhibitor / Poly(ethylene terephthalate) hydrolase

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