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 | 6 |
Details | binding site for residue ZN A 301 |
Chain | Residue |
A | ASP120 |
A | CYS199 |
A | HIS241 |
A | ZN302 |
A | NO3304 |
A | HOH431 |
site_id | AC2 |
Number of Residues | 5 |
Details | binding site for residue ZN A 302 |
Chain | Residue |
A | ZN301 |
A | HOH431 |
A | HIS116 |
A | HIS118 |
A | HIS180 |
site_id | AC3 |
Number of Residues | 8 |
Details | binding site for residue EDO A 303 |
Chain | Residue |
A | THR138 |
A | LEU140 |
A | THR141 |
A | ILE159 |
A | TYR175 |
A | ASP183 |
A | NO3308 |
A | HOH416 |
site_id | AC4 |
Number of Residues | 9 |
Details | binding site for residue NO3 A 304 |
Chain | Residue |
A | HIS180 |
A | CYS199 |
A | ARG202 |
A | GLY210 |
A | ASN211 |
A | HIS241 |
A | ZN301 |
A | HOH458 |
A | HOH501 |
site_id | AC5 |
Number of Residues | 6 |
Details | binding site for residue NO3 A 305 |
Chain | Residue |
A | LYS49 |
A | THR52 |
A | THR52 |
A | GLY53 |
A | GLU77 |
A | EDO315 |
site_id | AC6 |
Number of Residues | 7 |
Details | binding site for residue NO3 A 306 |
Chain | Residue |
A | ASN90 |
A | ASP91 |
A | GLY123 |
A | HOH403 |
A | HOH404 |
A | HOH410 |
A | HOH506 |
site_id | AC7 |
Number of Residues | 4 |
Details | binding site for residue EDO A 307 |
Chain | Residue |
A | ALA215 |
A | ASN216 |
A | LEU217 |
A | GLY218 |
site_id | AC8 |
Number of Residues | 9 |
Details | binding site for residue NO3 A 308 |
Chain | Residue |
A | THR138 |
A | ASP139 |
A | LEU140 |
A | LEU157 |
A | ASN158 |
A | ILE159 |
A | SER160 |
A | EDO303 |
A | HOH454 |
site_id | AC9 |
Number of Residues | 3 |
Details | binding site for residue NO3 A 309 |
Chain | Residue |
A | ARG202 |
A | HIS241 |
A | LYS251 |
site_id | AD1 |
Number of Residues | 4 |
Details | binding site for residue NO3 A 310 |
Chain | Residue |
A | LYS61 |
A | ASN90 |
A | HOH407 |
A | HOH466 |
site_id | AD2 |
Number of Residues | 5 |
Details | binding site for residue NO3 A 311 |
Chain | Residue |
A | ILE69 |
A | ARG70 |
A | HIS241 |
A | HOH408 |
A | HOH479 |
site_id | AD3 |
Number of Residues | 6 |
Details | binding site for residue EDO A 312 |
Chain | Residue |
A | VAL62 |
A | PRO64 |
A | PRO65 |
A | TRP66 |
A | GLY67 |
A | PRO232 |
site_id | AD4 |
Number of Residues | 6 |
Details | binding site for residue EDO A 313 |
Chain | Residue |
A | THR52 |
A | GLY53 |
A | GLU77 |
A | ARG78 |
A | GLU189 |
A | HOH418 |
site_id | AD5 |
Number of Residues | 4 |
Details | binding site for residue EDO A 314 |
Chain | Residue |
A | ASP91 |
A | ALA92 |
A | ALA95 |
A | HOH426 |
site_id | AD6 |
Number of Residues | 6 |
Details | binding site for residue EDO A 315 |
Chain | Residue |
A | LYS49 |
A | LEU50 |
A | GLY51 |
A | LYS107 |
A | NO3305 |
A | HOH474 |
site_id | AD7 |
Number of Residues | 4 |
Details | binding site for residue EDO A 316 |
Chain | Residue |
A | ASN68 |
A | GLN235 |
A | GLY246 |
A | ARG247 |
site_id | AD8 |
Number of Residues | 5 |
Details | binding site for residue FMT A 317 |
Chain | Residue |
A | MET56 |
A | ARG70 |
A | LYS243 |
A | PRO244 |
A | HOH453 |
site_id | AD9 |
Number of Residues | 6 |
Details | binding site for residue NO3 A 318 |
Chain | Residue |
A | LYS251 |
A | TYR255 |
A | HOH464 |
A | HOH468 |
A | SER208 |
A | GLY210 |
site_id | AE1 |
Number of Residues | 6 |
Details | binding site for residue PO4 A 319 |
Chain | Residue |
A | LYS154 |
A | LYS154 |
A | LYS154 |
A | HOH405 |
A | HOH405 |
A | HOH405 |
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 | |