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Structure paper

TitleStructural study reveals the temperature-dependent conformational flexibility of Tk-PTP, a protein tyrosine phosphatase from Thermococcus kodakaraensis KOD1
Journal, issue, pagesPLoS ONE, Vol. 13, Page e0197635-e0197635, Year 2018
Publish dateJan 17, 2018 (structure data deposition date)
AuthorsYun, H.Y. / Lee, J. / Kim, H. / Ryu, H. / Shin, H.C. / Oh, B.H. / Ku, B. / Kim, S.J.
External linksPLoS ONE / PubMed:29791483
MethodsX-ray diffraction
Resolution1.703 - 2.3 Å
Structure data

PDB-5z59:
Crystal structure of Tk-PTP in the inactive form
Method: X-RAY DIFFRACTION / Resolution: 1.703 Å

PDB-5z5a:
Crystal structure of Tk-PTP in the active form
Method: X-RAY DIFFRACTION / Resolution: 1.8 Å

PDB-5z5b:
Crystal structure of Tk-PTP in the G95A mutant form
Method: X-RAY DIFFRACTION / Resolution: 2.3 Å

Chemicals

ChemComp-HOH:
WATER

ChemComp-VN3:
VANADATE ION

ChemComp-CL:
Unknown entry

ChemComp-FMT:
FORMIC ACID

Source
  • thermococcus kodakarensis (strain atcc baa-918 / jcm 12380 / kod1) (archaea)
  • thermococcus kodakarensis kod1 (archaea)
KeywordsHYDROLASE / tyrosine phosphatase

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