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Structure paper

TitleHeat induces end to end repetitive association in P. furiosus L-asparaginase which enables its thermophilic property.
Journal, issue, pagesSci Rep, Vol. 10, Page 21702-21702, Year 2020
Publish dateMay 23, 2016 (structure data deposition date)
AuthorsSharma, P. / Tomar, R. / Yadav, S.S. / Badmalia, M.D. / Nath, S.K. / Kundu, B.
External linksSci Rep / PubMed:33303914
MethodsX-ray diffraction
Resolution2.039 - 2.61 Å
Structure data

PDB-5b5u:
Crystal structure of truncated Pyrococcus furiosus L-asparaginase with peptide
Method: X-RAY DIFFRACTION / Resolution: 2.61 Å

PDB-5b74:
Crystal structure of conjoined Pyrococcus furiosus L-asparaginase with peptide
Method: X-RAY DIFFRACTION / Resolution: 2.039 Å

PDB-5cbp:
Crystal Structure of Conjoint Pyrococcus furiosus L-asparaginase at 37 degree C
Method: X-RAY DIFFRACTION / Resolution: 2.358 Å

Chemicals

ChemComp-ASP:
ASPARTIC ACID

ChemComp-CL:
Unknown entry

ChemComp-IPA:
ISOPROPYL ALCOHOL / alkaloid*YM

ChemComp-GOL:
GLYCEROL

ChemComp-HOH:
WATER

ChemComp-FLC:
CITRATE ANION

Source
  • pyrococcus furiosus dsm 3638 (archaea)
  • pyrococcus furiosus (archaea)
KeywordsHYDROLASE / Truncated Pyrococcus furiosus L-asparaginase / Linkerless

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