EC Number   |
|---|
   3.5.2.B2 | homology modeling and molecular docking. The active site is located in the middle of the core structure, the catalytic triad is constituted by residues S171, S195, C145 |
| 3.5.2.B2 | molecular modeling. Structure does not show similartity to the domain structure of known gamma-lactamases, leading to gamma lactamase type II |
| 3.5.2.B2 | purified apo-form, (+)-gamma-lactam bound, and (-)-gamma-lactam bound forms of the enzyme, X-ray diffraction structure determination and analysis at 1.79-2.05 A resolution |
| 3.5.2.B2 | sitting drop vapor diffusion method at 20°C, crystal structures of the apo-form, (+)-gamma-lactam bound, and (-)-gamma-lactam bound forms of the enzyme |
