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 | 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 | 0071555 | biological_process | cell wall organization |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | binding site for residue SO4 A 301 |
| Chain | Residue |
| A | SER184 |
| A | GLU185 |
| A | ARG186 |
| A | HOH417 |
| A | HOH478 |
| B | ASN58 |
| site_id | AC2 |
| Number of Residues | 9 |
| Details | binding site for residue SO4 A 302 |
| Chain | Residue |
| A | GLY210 |
| A | TYR211 |
| A | ARG250 |
| A | HOH446 |
| A | HOH455 |
| A | HOH467 |
| A | SER70 |
| A | SER118 |
| A | THR209 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | binding site for residue SO4 A 303 |
| Chain | Residue |
| A | ASN48 |
| A | LYS51 |
| A | ASN231 |
| A | HOH407 |
| A | HOH409 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | binding site for residue SO4 A 304 |
| Chain | Residue |
| A | GLN98 |
| A | ARG100 |
| A | GLN124 |
| A | GOL305 |
| A | HOH419 |
| A | HOH527 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | binding site for residue GOL A 305 |
| Chain | Residue |
| A | VAL120 |
| A | GLN124 |
| A | SO4304 |
| A | HOH419 |
| site_id | AC6 |
| Number of Residues | 10 |
| Details | binding site for residue GOL A 306 |
| Chain | Residue |
| A | LYS39 |
| A | SER40 |
| A | GLN41 |
| A | HIS140 |
| A | ASP143 |
| A | GLU147 |
| A | PRO242 |
| A | GOL308 |
| A | HOH468 |
| B | LYS39 |
| site_id | AC7 |
| Number of Residues | 7 |
| Details | binding site for residue GOL A 307 |
| Chain | Residue |
| A | ASN32 |
| A | PHE35 |
| A | GLN41 |
| A | GLY42 |
| A | ASN58 |
| A | HOH404 |
| A | HOH462 |
| site_id | AC8 |
| Number of Residues | 10 |
| Details | binding site for residue GOL A 308 |
| Chain | Residue |
| A | LYS39 |
| A | SER40 |
| A | HIS140 |
| A | MET239 |
| A | MET241 |
| A | THR243 |
| A | GLY246 |
| A | GOL306 |
| A | HOH459 |
| A | HOH465 |
| site_id | AC9 |
| Number of Residues | 2 |
| Details | binding site for residue CL A 309 |
| Chain | Residue |
| A | ARG206 |
| B | ARG206 |
| site_id | AD1 |
| Number of Residues | 10 |
| Details | binding site for residue SO4 B 301 |
| Chain | Residue |
| B | SER70 |
| B | SER118 |
| B | LYS208 |
| B | THR209 |
| B | GLY210 |
| B | TYR211 |
| B | ARG250 |
| B | HOH430 |
| B | HOH475 |
| B | HOH492 |
| site_id | AD2 |
| Number of Residues | 6 |
| Details | binding site for residue SO4 B 302 |
| Chain | Residue |
| B | ASN48 |
| B | LYS51 |
| B | ASN231 |
| B | HOH403 |
| B | HOH455 |
| B | HOH486 |
| site_id | AD3 |
| Number of Residues | 5 |
| Details | binding site for residue SO4 B 303 |
| Chain | Residue |
| B | LYS60 |
| B | SER184 |
| B | GLU185 |
| B | HOH405 |
| B | HOH489 |
| site_id | AD4 |
| Number of Residues | 6 |
| Details | binding site for residue GOL B 304 |
| Chain | Residue |
| B | LYS39 |
| B | SER40 |
| B | ASP240 |
| B | ASP245 |
| B | GLY246 |
| B | HOH406 |
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 | |
