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TitleConformational flexibility of PL12 family heparinases: structure and substrate specificity of heparinase III from Bacteroides thetaiotaomicron (BT4657).
Journal, issue, pagesGlycobiology, Vol. 27, Page 176-187, Year 2017
Publish dateApr 28, 2016 (structure data deposition date)
AuthorsUlaganathan, T. / Shi, R. / Yao, D. / Gu, R.X. / Garron, M.L. / Cherney, M. / Tieleman, D.P. / Sterner, E. / Li, G. / Li, L. ...Ulaganathan, T. / Shi, R. / Yao, D. / Gu, R.X. / Garron, M.L. / Cherney, M. / Tieleman, D.P. / Sterner, E. / Li, G. / Li, L. / Linhardt, R.J. / Cygler, M.
External linksGlycobiology / PubMed:27621378
MethodsX-ray diffraction
Resolution1.854 - 2.4 Å
Structure data

PDB-5jmd:
Heparinase III-BT4657 gene product, Methylated Lysines
Method: X-RAY DIFFRACTION / Resolution: 2.4 Å

PDB-5jmf:
Heparinase III-BT4657 gene product
Method: X-RAY DIFFRACTION / Resolution: 1.854 Å

Chemicals

ChemComp-MG:
Unknown entry

ChemComp-HOH:
WATER

ChemComp-GOL:
GLYCEROL

ChemComp-TRS:
2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL / pH buffer*YM

Source
  • bacteroides thetaiotaomicron (bacteria)
KeywordsLYASE / PL12 / HeparinaseIII / BT4657 gene product / Bacteroides thetaiotaomicron

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