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TitleStructural basis for branching-enzyme activity of glycoside hydrolase family 57: Structure and stability studies of a novel branching enzyme from the hyperthermophilic archaeon Thermococcus Kodakaraensis KOD1.
Journal, issue, pagesProteins, Vol. 79, Page 547-557, Year 2011
Publish dateMay 28, 2010 (structure data deposition date)
AuthorsSantos, C.R. / Tonoli, C.C. / Trindade, D.M. / Betzel, C. / Takata, H. / Kuriki, T. / Kanai, T. / Imanaka, T. / Arni, R.K. / Murakami, M.T.
External linksProteins / PubMed:21104698
MethodsX-ray diffraction
Resolution1.87 - 2.89 Å
Structure data

PDB-3n8t:
Native structure of TK1436, a GH57 branching enzyme from hyperthermophilic archaeon Thermococcus kodakaraensis
Method: X-RAY DIFFRACTION / Resolution: 2.4 Å

PDB-3n92:
Crystal structure of TK1436, a GH57 branching enzyme from hyperthermophilic archaeon Thermococcus kodakaraensis, in complex with glucose
Method: X-RAY DIFFRACTION / Resolution: 2.89 Å

PDB-3n98:
Crystal structure of TK1436, a GH57 branching enzyme from hyperthermophilic archaeon Thermococcus kodakaraensis, in complex with glucose and additives
Method: X-RAY DIFFRACTION / Resolution: 1.87 Å

Chemicals

ChemComp-PEG:
DI(HYDROXYETHYL)ETHER

ChemComp-PG4:
TETRAETHYLENE GLYCOL / precipitant*YM

ChemComp-HOH:
WATER

ChemComp-BGC:
beta-D-glucopyranose

ChemComp-GOL:
GLYCEROL

ChemComp-DIO:
1,4-DIETHYLENE DIOXIDE

Source
  • thermococcus kodakarensis (archaea)
KeywordsTRANSFERASE / GH57 family member / branching enzyme

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