Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0008270 | molecular_function | zinc ion binding |
A | 0008800 | molecular_function | beta-lactamase activity |
A | 0017001 | biological_process | antibiotic catabolic process |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 4 |
Details | binding site for residue ZN A 301 |
Chain | Residue |
A | HIS116 |
A | HIS118 |
A | HIS180 |
A | X8Z304 |
site_id | AC2 |
Number of Residues | 4 |
Details | binding site for residue ZN A 302 |
Chain | Residue |
A | ASP120 |
A | CYS199 |
A | HIS241 |
A | X8Z304 |
site_id | AC3 |
Number of Residues | 7 |
Details | binding site for residue EDO A 303 |
Chain | Residue |
A | THR141 |
A | ILE159 |
A | SER160 |
A | TYR175 |
A | ASP183 |
A | HOH423 |
A | THR138 |
site_id | AC4 |
Number of Residues | 11 |
Details | binding site for residue X8Z A 304 |
Chain | Residue |
A | ILE69 |
A | HIS118 |
A | ASP120 |
A | HIS180 |
A | GLY210 |
A | ASN211 |
A | HIS241 |
A | LYS251 |
A | ZN301 |
A | ZN302 |
A | HOH412 |
site_id | AC5 |
Number of Residues | 6 |
Details | binding site for residue NA A 305 |
Chain | Residue |
A | ASP91 |
A | GLY123 |
A | HOH427 |
A | HOH458 |
A | HOH502 |
A | HOH527 |
site_id | AC6 |
Number of Residues | 5 |
Details | binding site for residue NA A 306 |
Chain | Residue |
A | GLY190 |
A | ASN193 |
A | HOH468 |
A | HOH526 |
A | HOH533 |
site_id | AC7 |
Number of Residues | 2 |
Details | binding site for residue FMT A 307 |
site_id | AC8 |
Number of Residues | 5 |
Details | binding site for residue FMT A 308 |
Chain | Residue |
A | MET56 |
A | ARG70 |
A | LYS243 |
A | PRO244 |
A | HOH421 |
site_id | AC9 |
Number of Residues | 2 |
Details | binding site for residue CL A 309 |
Chain | Residue |
A | HIS118 |
A | SER119 |
site_id | AD1 |
Number of Residues | 4 |
Details | binding site for residue CL A 310 |
Chain | Residue |
A | ASN90 |
A | ASP91 |
A | ALA92 |
A | HOH546 |
site_id | AD2 |
Number of Residues | 3 |
Details | binding site for residue CL A 311 |
Chain | Residue |
A | LYS154 |
A | LYS154 |
A | LYS154 |
site_id | AD3 |
Number of Residues | 1 |
Details | binding site for residue CL A 312 |
Functional Information from PROSITE/UniProt
site_id | PS00743 |
Number of Residues | 20 |
Details | BETA_LACTAMASE_B_1 Beta-lactamases class B signature 1. IhTHaHSDkmGGmdalhml.G |
Chain | Residue | Details |
A | ILE113-GLY132 | |