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TitleCrystal Structure of Escherichia coli Thioesterase I/Protease I/Lysophospholipase L1: Consensus Sequence Blocks Constitute the Catalytic Center of SGNH-hydrolases through a Conserved Hydrogen Bond Network
Journal, issue, pagesJ. Mol. Biol., Vol. 330, Page 539-551, Year 2003
Publish dateMar 27, 2002 (structure data deposition date)
AuthorsLo, Y.-C. / Lin, S.-C. / Shaw, J.-F. / Liaw, Y.-C.
External linksJ. Mol. Biol. / PubMed:12842470
MethodsX-ray diffraction
Resolution1.9 - 2 Å
Structure data

PDB-1ivn:
E.coli Thioesterase I/Protease I/Lysophospholiase L1
Method: X-RAY DIFFRACTION / Resolution: 1.9 Å

PDB-1j00:
E. coli Thioesterase I/Protease I/Lysophospholipase L1 in complexed with diethyl phosphono moiety
Method: X-RAY DIFFRACTION / Resolution: 2 Å

PDB-1jrl:
Crystal structure of E. coli Lysophospholiase L1/Acyl-CoA Thioesterase I/Protease I L109P mutant
Method: X-RAY DIFFRACTION / Resolution: 1.95 Å

Chemicals

ChemComp-SO4:
SULFATE ION

ChemComp-GOL:
GLYCEROL

ChemComp-HOH:
WATER

ChemComp-IMD:
IMIDAZOLE

Source
  • escherichia coli (E. coli)
KeywordsHYDROLASE / Protease

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