Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0008658 | molecular_function | penicillin binding |
| A | 0008800 | molecular_function | beta-lactamase activity |
| A | 0017001 | biological_process | antibiotic catabolic process |
| B | 0008658 | molecular_function | penicillin binding |
| B | 0008800 | molecular_function | beta-lactamase activity |
| B | 0017001 | biological_process | antibiotic catabolic process |
| C | 0008658 | molecular_function | penicillin binding |
| C | 0008800 | molecular_function | beta-lactamase activity |
| C | 0017001 | biological_process | antibiotic catabolic process |
| D | 0008658 | molecular_function | penicillin binding |
| D | 0008800 | molecular_function | beta-lactamase activity |
| D | 0017001 | biological_process | antibiotic catabolic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 13 |
| Details | binding site for residue DWZ A 301 |
| Chain | Residue |
| A | ALA69 |
| A | TYR211 |
| A | ARG250 |
| A | HOH407 |
| A | HOH409 |
| A | SER70 |
| A | KCX73 |
| A | ILE102 |
| A | THR104 |
| A | TYR117 |
| A | VAL120 |
| A | LEU158 |
| A | GLY210 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | binding site for residue EDO A 302 |
| Chain | Residue |
| A | LEU81 |
| A | SER184 |
| A | ARG186 |
| A | SER187 |
| A | HOH492 |
| A | HOH556 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | binding site for residue EDO A 303 |
| Chain | Residue |
| A | ASP229 |
| A | ASP230 |
| A | HOH532 |
| A | HOH542 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | binding site for residue EDO A 304 |
| Chain | Residue |
| A | TYR177 |
| A | GLU227 |
| A | VAL232 |
| A | HOH420 |
| A | HOH437 |
| site_id | AC5 |
| Number of Residues | 2 |
| Details | binding site for residue CL A 305 |
| Chain | Residue |
| A | ARG206 |
| A | HOH592 |
| site_id | AC6 |
| Number of Residues | 18 |
| Details | binding site for residue DWZ B 301 |
| Chain | Residue |
| B | ALA69 |
| B | SER70 |
| B | THR104 |
| B | TYR117 |
| B | SER118 |
| B | VAL120 |
| B | GLY210 |
| B | TYR211 |
| B | LEU247 |
| B | ARG250 |
| B | HOH424 |
| B | HOH436 |
| B | HOH489 |
| B | HOH503 |
| B | HOH510 |
| B | HOH529 |
| B | HOH542 |
| B | HOH619 |
| site_id | AC7 |
| Number of Residues | 7 |
| Details | binding site for residue EDO B 302 |
| Chain | Residue |
| B | VAL120 |
| B | GLN124 |
| B | ARG214 |
| B | HOH414 |
| C | ASP159 |
| C | ARG214 |
| C | EDO302 |
| site_id | AC8 |
| Number of Residues | 3 |
| Details | binding site for residue EDO B 303 |
| Chain | Residue |
| B | SER136 |
| B | ILE149 |
| B | GLY151 |
| site_id | AC9 |
| Number of Residues | 7 |
| Details | binding site for residue EDO B 304 |
| Chain | Residue |
| B | LYS39 |
| B | SER40 |
| B | ASP240 |
| B | MET241 |
| B | PRO242 |
| B | HOH451 |
| B | HOH464 |
| site_id | AD1 |
| Number of Residues | 4 |
| Details | binding site for residue EDO B 305 |
| Chain | Residue |
| B | HIS109 |
| B | ASN110 |
| B | HOH446 |
| B | HOH492 |
| site_id | AD2 |
| Number of Residues | 5 |
| Details | binding site for residue EDO B 306 |
| Chain | Residue |
| B | LEU81 |
| B | SER184 |
| B | ARG186 |
| B | SER187 |
| B | HOH586 |
| site_id | AD3 |
| Number of Residues | 11 |
| Details | binding site for residue EDO C 302 |
| Chain | Residue |
| B | GLN124 |
| B | SER155 |
| B | LEU158 |
| B | ASP159 |
| B | ARG214 |
| B | EDO302 |
| C | SER155 |
| C | LEU158 |
| C | ASP159 |
| C | ARG214 |
| C | EDO304 |
| site_id | AD4 |
| Number of Residues | 7 |
| Details | binding site for residue EDO C 303 |
| Chain | Residue |
| C | ALA65 |
| C | PHE66 |
| C | PRO217 |
| C | HOH408 |
| C | HOH434 |
| C | HOH452 |
| C | HOH522 |
| site_id | AD5 |
| Number of Residues | 7 |
| Details | binding site for residue EDO C 304 |
| Chain | Residue |
| B | ASP159 |
| B | ARG214 |
| C | GLN124 |
| C | ARG214 |
| C | EDO302 |
| C | HOH423 |
| C | HOH519 |
| site_id | AD6 |
| Number of Residues | 6 |
| Details | binding site for residue EDO C 305 |
| Chain | Residue |
| C | SER40 |
| C | MET239 |
| C | ASP240 |
| C | PRO242 |
| C | HOH407 |
| C | HOH426 |
| site_id | AD7 |
| Number of Residues | 5 |
| Details | binding site for residue EDO C 306 |
| Chain | Residue |
| C | TYR177 |
| C | GLU227 |
| C | VAL232 |
| C | HOH468 |
| C | HOH475 |
| site_id | AD8 |
| Number of Residues | 6 |
| Details | binding site for residue EDO D 302 |
| Chain | Residue |
| B | ASP148 |
| B | HOH413 |
| D | ARG61 |
| D | PRO217 |
| D | ASP240 |
| D | HOH428 |
| site_id | AD9 |
| Number of Residues | 6 |
| Details | binding site for residue EDO D 303 |
| Chain | Residue |
| D | LEU81 |
| D | SER184 |
| D | ARG186 |
| D | SER187 |
| D | HOH449 |
| D | HOH553 |
| site_id | AE1 |
| Number of Residues | 5 |
| Details | binding site for residue EDO D 304 |
| Chain | Residue |
| D | HIS90 |
| D | ILE112 |
| D | HOH423 |
| D | HOH457 |
| D | HOH506 |
| site_id | AE2 |
| Number of Residues | 6 |
| Details | binding site for residue EDO D 305 |
| Chain | Residue |
| D | TYR177 |
| D | GLU227 |
| D | VAL232 |
| D | HOH427 |
| D | HOH436 |
| D | HOH462 |
| site_id | AE3 |
| Number of Residues | 6 |
| Details | binding site for residue EDO D 306 |
| Chain | Residue |
| D | SER40 |
| D | ASP240 |
| D | MET241 |
| D | PRO242 |
| D | HOH430 |
| D | HOH434 |
| site_id | AE4 |
| Number of Residues | 3 |
| Details | binding site for residue EDO D 307 |
| Chain | Residue |
| D | HIS109 |
| D | ASN110 |
| D | HOH566 |
| site_id | AE5 |
| Number of Residues | 21 |
| Details | binding site for Di-peptide GYJ C 301 and SER C 70 |
| Chain | Residue |
| C | PRO68 |
| C | ALA69 |
| C | THR71 |
| C | PHE72 |
| C | LYS73 |
| C | THR104 |
| C | TYR117 |
| C | SER118 |
| C | VAL120 |
| C | LYS208 |
| C | THR209 |
| C | GLY210 |
| C | TYR211 |
| C | LEU247 |
| C | ARG250 |
| C | HOH456 |
| C | HOH459 |
| C | HOH483 |
| C | HOH547 |
| C | HOH574 |
| C | HOH599 |
| site_id | AE6 |
| Number of Residues | 22 |
| Details | binding site for Di-peptide GYJ D 301 and SER D 70 |
| Chain | Residue |
| D | PRO68 |
| D | ALA69 |
| D | THR71 |
| D | PHE72 |
| D | KCX73 |
| D | THR104 |
| D | TRP105 |
| D | TYR117 |
| D | SER118 |
| D | VAL120 |
| D | LEU158 |
| D | LYS208 |
| D | THR209 |
| D | GLY210 |
| D | TYR211 |
| D | ARG250 |
| D | HOH426 |
| D | HOH437 |
| D | HOH587 |
| D | HOH595 |
| D | HOH612 |
| D | HOH717 |
Functional Information from PROSITE/UniProt
| site_id | PS00337 |
| Number of Residues | 11 |
| Details | BETA_LACTAMASE_D Beta-lactamase class-D active site. PaSTFKIPnSL |
| Chain | Residue | Details |
| A | PRO68-LEU78 | |
| B | PRO68-LEU78 | |
