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 and M0258 entries) to effect beta-lactam cleavage (PMID10508665). This hit refers to L1 metallo-beta-lactamase from Stenotrophomonas maltophilia which is a unique example among beta-lactamases in that it is tetrameric.
ZN 270 A IN THE RESTING STATE ENZYME
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Representative PDB structure for ZN 270 A in the resting state enzyme | |
| PDB code | 1sml | |
| Metal Type in the PDB | zinc | |
| Residue name of the metal in the PDB | ZN | |
| Residue number of the metal in the PDB | 270 | |
| 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 | NOTES ON PDB: | |
| First Coordination Sphere | ||||||
| Ligand Type | Ligand Identity | Residue In MACiE | Donors | Bind Mode | Catalytic? | Notes |
| residue | ASP 88 A | ASP 88 A | OD2 | monodentate | No | - |
| residue | HIS 89 A | HIS 89 A | NE2 | monodentate | No | - |
| residue | HIS 225 A | HIS 225 A | NE2 | monodentate | No | - |
| water | HOH 528 A | - | O | monodentate | No | - |
| water | HOH 568 A | - | O | monodentate | No | - |