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Structure paper

TitleInitial insight into the function of the lysosomal 66.3 kDa protein from mouse by means of X-ray crystallography
Journal, issue, pagesBmc Struct. Biol., Vol. 9, Page 56-56, Year 2009
Publish dateDec 8, 2008 (structure data deposition date)
AuthorsLakomek, K. / Dickmanns, A. / Kettwig, M. / Urlaub, H. / Ficner, R. / Luebke, T.
External linksBmc Struct. Biol. / PubMed:19706171
MethodsX-ray diffraction
Resolution1.8 - 2.8 Å
Structure data

PDB-3fgr:
Two chain form of the 66.3 kDa protein at 1.8 Angstroem
Method: X-RAY DIFFRACTION / Resolution: 1.8 Å

PDB-3fgt:
Two chain form of the 66.3 kDa protein from mouse lacking the linker peptide
Method: X-RAY DIFFRACTION / Resolution: 2.4 Å

PDB-3fgw:
One chain form of the 66.3 kDa protein
Method: X-RAY DIFFRACTION / Resolution: 2.8 Å

Chemicals

ChemComp-NAG:
2-acetamido-2-deoxy-beta-D-glucopyranose

ChemComp-GOL:
GLYCEROL

ChemComp-ACT:
ACETATE ION

ChemComp-XE:
XENON

ChemComp-NA:
Unknown entry

ChemComp-HOH:
WATER

ChemComp-PG4:
TETRAETHYLENE GLYCOL / precipitant*YM

ChemComp-7PE:
2-(2-(2-(2-(2-(2-ETHOXYETHOXY)ETHOXY)ETHOXY)ETHOXY)ETHOXY)ETHANOL

ChemComp-IOD:
IODIDE ION

Source
  • mus musculus (house mouse)
KeywordsHYDROLASE / alpha beta / glycosylated / disulphide bonds / N-terminal nucleophile hydrolase fold / two chain form / Glycoprotein / Lipid degradation / Lysosome / N-terminal hydrolase fold / occupied pocket / one chain form

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