Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005886 | cellular_component | plasma membrane |
| 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 | 0005886 | cellular_component | plasma membrane |
| 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 | 0005886 | cellular_component | plasma membrane |
| 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 | 0005886 | cellular_component | plasma membrane |
| 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 | 10 |
| Details | binding site for residue 2RG A 301 |
| Chain | Residue |
| A | ALA66 |
| A | HOH536 |
| A | SER67 |
| A | SER115 |
| A | VAL117 |
| A | LEU155 |
| A | THR206 |
| A | GLY207 |
| A | TRP208 |
| A | ARG247 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | binding site for residue EDO A 302 |
| Chain | Residue |
| A | ASN85 |
| A | HIS87 |
| A | HOH405 |
| D | LEU175 |
| D | ASN176 |
| D | LYS182 |
| site_id | AC3 |
| Number of Residues | 8 |
| Details | binding site for residue EDO B 302 |
| Chain | Residue |
| B | GLN113 |
| B | THR194 |
| B | SER204 |
| B | LYS205 |
| B | THR206 |
| B | HOH412 |
| B | HOH435 |
| B | HOH466 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | binding site for residue EDO B 303 |
| Chain | Residue |
| B | VAL89 |
| B | ASP105 |
| B | HOH516 |
| C | THR227 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | binding site for residue EDO C 302 |
| Chain | Residue |
| B | LEU186 |
| B | LYS189 |
| B | GLU190 |
| C | GLU86 |
| C | GLU190 |
| C | HOH513 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | binding site for residue EDO C 303 |
| Chain | Residue |
| B | GLU224 |
| B | GLU226 |
| B | HOH482 |
| C | THR107 |
| C | ARG109 |
| site_id | AC7 |
| Number of Residues | 8 |
| Details | binding site for residue EDO C 304 |
| Chain | Residue |
| C | GLU195 |
| C | TYR200 |
| C | VAL202 |
| C | TRP219 |
| C | THR252 |
| C | ILE261 |
| C | HOH516 |
| C | HOH594 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | binding site for residue EDO C 305 |
| Chain | Residue |
| C | GLU126 |
| D | GLU256 |
| D | GLY259 |
| D | ILE261 |
| D | GLY262 |
| D | HOH510 |
| site_id | AC9 |
| Number of Residues | 7 |
| Details | binding site for residue EDO C 306 |
| Chain | Residue |
| B | THR107 |
| B | ARG109 |
| C | GLU199 |
| C | GLU224 |
| C | GLU226 |
| C | HOH502 |
| C | HOH566 |
| site_id | AD1 |
| Number of Residues | 7 |
| Details | binding site for residue EDO C 307 |
| Chain | Residue |
| C | ALA36 |
| C | ASN38 |
| C | HOH411 |
| D | ARG58 |
| D | LYS61 |
| D | HOH409 |
| D | HOH537 |
| site_id | AD2 |
| Number of Residues | 7 |
| Details | binding site for residue EDO D 302 |
| Chain | Residue |
| A | THR107 |
| A | ARG109 |
| D | GLU199 |
| D | GLU224 |
| D | GLU226 |
| D | HOH468 |
| D | HOH503 |
| site_id | AD3 |
| Number of Residues | 4 |
| Details | binding site for residue EDO D 303 |
| Chain | Residue |
| A | HOH499 |
| D | THR107 |
| D | ARG109 |
| D | EDO306 |
| site_id | AD4 |
| Number of Residues | 3 |
| Details | binding site for residue EDO D 304 |
| Chain | Residue |
| D | GLY149 |
| D | ILE150 |
| D | HOH512 |
| site_id | AD5 |
| Number of Residues | 5 |
| Details | binding site for residue EDO D 305 |
| Chain | Residue |
| D | ARG131 |
| D | TYR135 |
| D | HOH509 |
| D | HOH555 |
| D | HOH562 |
| site_id | AD6 |
| Number of Residues | 7 |
| Details | binding site for residue EDO D 306 |
| Chain | Residue |
| A | PRO198 |
| A | HOH412 |
| D | ARG104 |
| D | GLY110 |
| D | 2RG301 |
| D | EDO303 |
| D | HOH558 |
| site_id | AD7 |
| Number of Residues | 15 |
| Details | binding site for Di-peptide 2RG B 301 and SER B 67 |
| Chain | Residue |
| B | SER115 |
| B | VAL117 |
| B | LEU155 |
| B | LYS205 |
| B | THR206 |
| B | GLY207 |
| B | TRP208 |
| B | ARG247 |
| B | HOH559 |
| B | PRO65 |
| B | ALA66 |
| B | THR68 |
| B | PHE69 |
| B | KCX70 |
| B | GLN101 |
| site_id | AD8 |
| Number of Residues | 20 |
| Details | binding site for Di-peptide 2RG C 301 and SER C 67 |
| Chain | Residue |
| B | PRO198 |
| C | PRO65 |
| C | ALA66 |
| C | THR68 |
| C | PHE69 |
| C | KCX70 |
| C | MET99 |
| C | GLN101 |
| C | ARG104 |
| C | VAL114 |
| C | SER115 |
| C | VAL117 |
| C | LEU155 |
| C | LYS205 |
| C | THR206 |
| C | GLY207 |
| C | TRP208 |
| C | ARG247 |
| C | HOH418 |
| C | HOH583 |
| site_id | AD9 |
| Number of Residues | 20 |
| Details | binding site for Di-peptide 2RG D 301 and SER D 67 |
| Chain | Residue |
| A | PRO198 |
| D | PRO65 |
| D | ALA66 |
| D | THR68 |
| D | PHE69 |
| D | KCX70 |
| D | MET99 |
| D | GLN101 |
| D | ARG104 |
| D | VAL114 |
| D | SER115 |
| D | VAL117 |
| D | LEU155 |
| D | LYS205 |
| D | THR206 |
| D | GLY207 |
| D | TRP208 |
| D | ARG247 |
| D | EDO306 |
| D | HOH402 |
Functional Information from PROSITE/UniProt
| site_id | PS00337 |
| Number of Residues | 11 |
| Details | BETA_LACTAMASE_D Beta-lactamase class-D active site. PaSTFKIPnAI |
| Chain | Residue | Details |
| A | PRO65-ILE75 | |
