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Structure paper

TitleStructural bases of stability-function tradeoffs in enzymes.
Journal, issue, pagesJ. Mol. Biol., Vol. 321, Page 285-296, Year 2002
Publish dateFeb 9, 2002 (structure data deposition date)
AuthorsBeadle, B.M. / Shoichet, B.K.
External linksJ. Mol. Biol. / PubMed:12144785
MethodsX-ray diffraction
Resolution1.5 - 1.9 Å
Structure data

PDB-1l0d:
X-ray Crystal Structure of AmpC S64D Mutant beta-Lactamase
Method: X-RAY DIFFRACTION / Resolution: 1.53 Å

PDB-1l0e:
X-ray Crystal Structure of AmpC K67Q Mutant beta-Lactamase
Method: X-RAY DIFFRACTION / Resolution: 1.9 Å

PDB-1l0f:
X-ray Crystal Structure of AmpC N152H Mutant beta-Lactamase
Method: X-RAY DIFFRACTION / Resolution: 1.66 Å

PDB-1l0g:
X-ray Crystal Structure of AmpC S64G Mutant beta-Lactamase
Method: X-RAY DIFFRACTION / Resolution: 1.5 Å

Chemicals

ChemComp-PO4:
PHOSPHATE ION

ChemComp-HOH:
WATER

Source
  • escherichia coli (E. coli)
KeywordsHYDROLASE / amide hydrolase / beta-lactamase / mutant enzyme

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