Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0008658 | molecular_function | penicillin binding |
| A | 0008800 | molecular_function | beta-lactamase activity |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0017001 | biological_process | antibiotic catabolic process |
| A | 0046677 | biological_process | response to antibiotic |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0071555 | biological_process | cell wall organization |
| B | 0008658 | molecular_function | penicillin binding |
| B | 0008800 | molecular_function | beta-lactamase activity |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0017001 | biological_process | antibiotic catabolic process |
| B | 0046677 | biological_process | response to antibiotic |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0071555 | biological_process | cell wall organization |
| C | 0008658 | molecular_function | penicillin binding |
| C | 0008800 | molecular_function | beta-lactamase activity |
| C | 0016787 | molecular_function | hydrolase activity |
| C | 0017001 | biological_process | antibiotic catabolic process |
| C | 0046677 | biological_process | response to antibiotic |
| C | 0046872 | molecular_function | metal ion binding |
| C | 0071555 | biological_process | cell wall organization |
| D | 0008658 | molecular_function | penicillin binding |
| D | 0008800 | molecular_function | beta-lactamase activity |
| D | 0016787 | molecular_function | hydrolase activity |
| D | 0017001 | biological_process | antibiotic catabolic process |
| D | 0046677 | biological_process | response to antibiotic |
| D | 0046872 | molecular_function | metal ion binding |
| D | 0071555 | biological_process | cell wall organization |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 8 |
| Details | binding site for residue GA6 A 301 |
| Chain | Residue |
| A | SER70 |
| A | SER118 |
| A | THR209 |
| A | GLY210 |
| A | TYR211 |
| A | SER244 |
| A | ARG250 |
| A | HOH401 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | binding site for residue EDO A 302 |
| Chain | Residue |
| A | THR167 |
| A | ILE170 |
| A | SER171 |
| A | ARG174 |
| A | TRP25 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | binding site for residue EDO A 303 |
| Chain | Residue |
| A | LYS94 |
| A | TRP95 |
| A | ASP96 |
| A | PRO121 |
| A | VAL122 |
| A | HOH485 |
| A | HOH560 |
| site_id | AC4 |
| Number of Residues | 7 |
| Details | binding site for residue EDO A 304 |
| Chain | Residue |
| A | TYR177 |
| A | GLU227 |
| A | VAL232 |
| A | HOH412 |
| A | HOH419 |
| C | HIS90 |
| C | HOH498 |
| site_id | AC5 |
| Number of Residues | 1 |
| Details | binding site for residue CL B 301 |
| site_id | AC6 |
| Number of Residues | 7 |
| Details | binding site for residue GA6 B 302 |
| Chain | Residue |
| B | SER70 |
| B | SER118 |
| B | THR209 |
| B | GLY210 |
| B | TYR211 |
| B | SER244 |
| B | ARG250 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | binding site for residue EDO B 303 |
| Chain | Residue |
| B | TYR177 |
| B | GLU227 |
| B | VAL232 |
| B | HOH431 |
| B | HOH445 |
| site_id | AC8 |
| Number of Residues | 7 |
| Details | binding site for residue EDO B 304 |
| Chain | Residue |
| B | LYS39 |
| B | SER40 |
| B | ASP240 |
| B | PRO242 |
| B | HOH401 |
| B | HOH417 |
| B | HOH443 |
| site_id | AC9 |
| Number of Residues | 2 |
| Details | binding site for residue EDO B 305 |
| Chain | Residue |
| B | ASN110 |
| B | HOH574 |
| site_id | AD1 |
| Number of Residues | 4 |
| Details | binding site for residue CL C 301 |
| Chain | Residue |
| A | ARG206 |
| A | HOH647 |
| C | ARG206 |
| C | HOH607 |
| site_id | AD2 |
| Number of Residues | 10 |
| Details | binding site for residue GA6 C 302 |
| Chain | Residue |
| C | SER70 |
| C | ILE102 |
| C | SER118 |
| C | THR209 |
| C | GLY210 |
| C | TYR211 |
| C | SER244 |
| C | ARG250 |
| C | HOH401 |
| C | HOH410 |
| site_id | AD3 |
| Number of Residues | 4 |
| Details | binding site for residue EDO C 303 |
| Chain | Residue |
| C | ILE170 |
| C | SER171 |
| C | ARG174 |
| C | HOH479 |
| site_id | AD4 |
| Number of Residues | 7 |
| Details | binding site for residue EDO C 304 |
| Chain | Residue |
| A | HIS90 |
| A | HOH434 |
| C | TYR177 |
| C | GLU227 |
| C | VAL232 |
| C | HOH418 |
| C | HOH500 |
| site_id | AD5 |
| Number of Residues | 4 |
| Details | binding site for residue EDO C 305 |
| Chain | Residue |
| C | PHE93 |
| C | LYS94 |
| C | TRP95 |
| C | ASP96 |
| site_id | AD6 |
| Number of Residues | 4 |
| Details | binding site for residue EDO D 301 |
| Chain | Residue |
| D | TYR177 |
| D | GLU227 |
| D | VAL232 |
| D | HOH452 |
| site_id | AD7 |
| Number of Residues | 5 |
| Details | binding site for residue EDO D 302 |
| Chain | Residue |
| D | LYS94 |
| D | TRP95 |
| D | ASP96 |
| D | HOH406 |
| D | HOH448 |
| site_id | AD8 |
| Number of Residues | 5 |
| Details | binding site for residue EDO D 303 |
| Chain | Residue |
| D | TRP47 |
| D | ILE170 |
| D | SER171 |
| D | ARG174 |
| D | HOH583 |
| site_id | AD9 |
| Number of Residues | 11 |
| Details | binding site for residue GA6 D 304 |
| Chain | Residue |
| D | ARG250 |
| D | HOH407 |
| D | HOH410 |
| D | HOH581 |
| D | SER70 |
| D | ILE102 |
| D | SER118 |
| D | THR209 |
| D | GLY210 |
| D | TYR211 |
| D | SER244 |
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 | |
