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TitleStructural Basis for the Role of Asp-120 in Metallo-beta-lactamases.
Journal, issue, pagesBiochemistry, Vol. 46, Page 10664-10674, Year 2007
Publish dateJul 5, 2007 (structure data deposition date)
AuthorsCrisp, J. / Conners, R. / Garrity, J.D. / Carenbauer, A.L. / Crowder, M.W. / Spencer, J.
External linksBiochemistry / PubMed:17715946
MethodsX-ray diffraction
Resolution1.76 - 2.25 Å
Structure data

PDB-2qin:
Stenotrophomonas maltophilia L1 Metallo-beta-Lactamase Asp-120 Cys mutant
Method: X-RAY DIFFRACTION / Resolution: 1.76 Å

PDB-2qjs:
Stenotrophomonas maltophilia L1 metallo-beta-lactamase Asp-120 Asn mutant
Method: X-RAY DIFFRACTION / Resolution: 2.25 Å

Chemicals

ChemComp-ZN:
Unknown entry

ChemComp-MG:
Unknown entry

ChemComp-HOH:
WATER

Source
  • stenotrophomonas maltophilia (bacteria)
KeywordsHYDROLASE / METALLO-BETA-LACTAMASE / BINUCLEAR / DINUCLEAR / dinculear / binculear

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