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TitleAn ultrahigh resolution structure of TEM-1 beta-lactamase suggests a role for Glu166 as the general base in acylation.
Journal, issue, pagesJ. Am. Chem. Soc., Vol. 124, Page 5333-5340, Year 2002
Publish dateJul 1, 2002 (structure data deposition date)
AuthorsMinasov, G. / Wang, X. / Shoichet, B.K.
External linksJ. Am. Chem. Soc. / PubMed:11996574
MethodsX-ray diffraction
Resolution0.85 Å
Structure data

PDB-1m40:
ULTRA HIGH RESOLUTION CRYSTAL STRUCTURE OF TEM-1
Method: X-RAY DIFFRACTION / Resolution: 0.85 Å

Chemicals

ChemComp-PO4:
PHOSPHATE ION

ChemComp-K:
Unknown entry

ChemComp-CB4:
PINACOL[[2-AMINO-ALPHA-(1-CARBOXY-1-METHYLETHOXYIMINO)-4-THIAZOLEACETYL]AMINO]METHANEBORONATE

ChemComp-HOH:
WATER

Source
  • escherichia coli (E. coli)
KeywordsHYDROLASE / BETA-LACTAMASE / ACYLATION MECHANISM

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