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 | 4 |
| Details | binding site for residue EDO A 301 |
| Chain | Residue |
| A | ASN143 |
| A | ASN145 |
| A | HOH448 |
| A | HOH503 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | binding site for residue EDO A 302 |
| Chain | Residue |
| A | GLU224 |
| A | GLU226 |
| A | HOH511 |
| C | THR107 |
| site_id | AC3 |
| Number of Residues | 20 |
| Details | binding site for residue DWZ A 303 |
| Chain | Residue |
| A | SER67 |
| A | KCX70 |
| A | MET99 |
| A | GLN101 |
| A | TRP102 |
| A | GLN113 |
| A | VAL114 |
| A | SER115 |
| A | VAL117 |
| A | LEU155 |
| A | GLY207 |
| A | TRP208 |
| A | ARG247 |
| A | HOH416 |
| A | HOH437 |
| A | HOH449 |
| A | HOH469 |
| A | HOH491 |
| C | PRO198 |
| A | ALA66 |
| site_id | AC4 |
| Number of Residues | 2 |
| Details | binding site for residue EDO A 304 |
| Chain | Residue |
| A | SER181 |
| A | LYS182 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | binding site for residue EDO A 305 |
| Chain | Residue |
| A | ARG160 |
| A | HOH470 |
| A | HOH522 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | binding site for residue EDO B 301 |
| Chain | Residue |
| B | ALA98 |
| B | HOH417 |
| B | HOH585 |
| B | HOH586 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | binding site for residue EDO B 303 |
| Chain | Residue |
| A | LYS84 |
| A | ASN85 |
| A | HOH429 |
| B | THR23 |
| B | GLU24 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | binding site for residue EDO B 304 |
| Chain | Residue |
| B | ASN143 |
| B | ASN145 |
| B | HOH449 |
| B | HOH474 |
| site_id | AC9 |
| Number of Residues | 3 |
| Details | binding site for residue EDO B 305 |
| Chain | Residue |
| B | ARG160 |
| B | HOH476 |
| B | HOH531 |
| site_id | AD1 |
| Number of Residues | 9 |
| Details | binding site for residue EDO C 301 |
| Chain | Residue |
| C | ALA36 |
| C | VAL37 |
| C | ASN38 |
| C | HOH402 |
| D | ASP55 |
| D | ALA57 |
| D | ARG58 |
| D | LYS61 |
| D | HOH410 |
| site_id | AD2 |
| Number of Residues | 7 |
| Details | binding site for residue EDO D 301 |
| Chain | Residue |
| B | THR107 |
| B | HOH468 |
| D | GLU199 |
| D | GLU224 |
| D | GLU226 |
| D | HOH445 |
| D | HOH553 |
| site_id | AD3 |
| Number of Residues | 4 |
| Details | binding site for residue EDO D 302 |
| Chain | Residue |
| C | THR252 |
| D | ARG131 |
| D | TYR135 |
| D | HOH429 |
| site_id | AD4 |
| Number of Residues | 3 |
| Details | binding site for residue EDO D 304 |
| Chain | Residue |
| D | LYS84 |
| D | ASN85 |
| D | HOH493 |
| site_id | AD5 |
| Number of Residues | 25 |
| Details | binding site for Di-peptide DWZ B 302 and SER B 67 |
| Chain | Residue |
| B | PRO65 |
| B | ALA66 |
| B | THR68 |
| B | PHE69 |
| B | KCX70 |
| B | MET99 |
| B | GLN101 |
| B | TRP102 |
| B | GLN113 |
| B | VAL114 |
| B | SER115 |
| B | VAL117 |
| B | LEU155 |
| B | LYS205 |
| B | THR206 |
| B | GLY207 |
| B | TRP208 |
| B | MET210 |
| B | ARG247 |
| B | HOH408 |
| B | HOH416 |
| B | HOH443 |
| B | HOH523 |
| B | HOH525 |
| D | PRO198 |
| site_id | AD6 |
| Number of Residues | 23 |
| Details | binding site for Di-peptide DWZ C 302 and SER C 67 |
| Chain | Residue |
| C | THR68 |
| C | PHE69 |
| C | KCX70 |
| C | MET99 |
| C | GLN101 |
| C | VAL114 |
| C | SER115 |
| C | VAL117 |
| C | LEU155 |
| C | LYS205 |
| C | THR206 |
| C | GLY207 |
| C | TRP208 |
| C | MET210 |
| C | LEU244 |
| C | ARG247 |
| C | HOH401 |
| C | HOH418 |
| C | HOH436 |
| C | HOH493 |
| C | HOH545 |
| C | PRO65 |
| C | ALA66 |
| site_id | AD7 |
| Number of Residues | 21 |
| Details | binding site for Di-peptide DWZ D 303 and SER D 67 |
| Chain | Residue |
| D | PRO65 |
| D | ALA66 |
| D | THR68 |
| D | PHE69 |
| D | KCX70 |
| D | MET99 |
| D | GLN101 |
| D | VAL114 |
| D | SER115 |
| D | VAL117 |
| D | LEU155 |
| D | LYS205 |
| D | THR206 |
| D | GLY207 |
| D | TRP208 |
| D | MET210 |
| D | ARG247 |
| D | HOH407 |
| D | HOH422 |
| D | HOH489 |
| D | HOH522 |
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 | |
