The enzyme catalyzes the hydrolysis of the C-N bond in beta-lactam compounds determining the inactivation of such antibiotics. Members of the beta-lactamase family have been grouped into four classes (A, B, C, D). Class B members employ either one (see M0016 entry) or two zinc ions in a dinuclear site (see M0015 entry) to effect beta-lactam cleavage (PMID10508665).
ZN 1 A IN THE RESTING STATE ENZYME
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Representative PDB structure for ZN 1 A in the resting state enzyme | |
| PDB code | 1znb | |
| Metal Type in the PDB | zinc | |
| Residue name of the metal in the PDB | ZN | |
| Residue number of the metal in the PDB | 1 | |
| Chain of the metal in the PDB | A | |
| Atom name of the metal in the PDB | ZN | |
| Download the coordinates file of the metal site | ||
| First Coordination Sphere | ||||||
| Ligand Type | Ligand Identity | Residue In MACiE | Donors | Bind Mode | Catalytic? | Notes |
| residue | HIS 99 A | HIS 99 A | NE2 | monodentate | No | - |
| residue | HIS 101 A | HIS 101 A | ND1 | monodentate | No | - |
| residue | HIS 162 A | HIS 162 A | NE2 | monodentate | No | - |
| water | HOH 1 _ | - | O | monodentate | No | This water is activated by the binding of the two zinc ions. |