4U0X
Structure of ADC-7 beta-lactamase in complex with boronic acid inhibitor S02030
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0008800 | molecular_function | beta-lactamase activity |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0017001 | biological_process | antibiotic catabolic process |
| A | 0030288 | cellular_component | outer membrane-bounded periplasmic space |
| A | 0046677 | biological_process | response to antibiotic |
| B | 0008800 | molecular_function | beta-lactamase activity |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0017001 | biological_process | antibiotic catabolic process |
| B | 0030288 | cellular_component | outer membrane-bounded periplasmic space |
| B | 0046677 | biological_process | response to antibiotic |
| C | 0008800 | molecular_function | beta-lactamase activity |
| C | 0016787 | molecular_function | hydrolase activity |
| C | 0017001 | biological_process | antibiotic catabolic process |
| C | 0030288 | cellular_component | outer membrane-bounded periplasmic space |
| C | 0046677 | biological_process | response to antibiotic |
| D | 0008800 | molecular_function | beta-lactamase activity |
| D | 0016787 | molecular_function | hydrolase activity |
| D | 0017001 | biological_process | antibiotic catabolic process |
| D | 0030288 | cellular_component | outer membrane-bounded periplasmic space |
| D | 0046677 | biological_process | response to antibiotic |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 10 |
| Details | binding site for residue ZXM B 401 |
| Chain | Residue |
| B | SER64 |
| B | HOH653 |
| B | GLN120 |
| B | TYR150 |
| B | ASN152 |
| B | GLY314 |
| B | SER315 |
| B | THR316 |
| B | ARG340 |
| B | HOH582 |
| site_id | AC2 |
| Number of Residues | 12 |
| Details | binding site for residue ZXM A 401 |
| Chain | Residue |
| A | SER64 |
| A | GLN120 |
| A | TYR150 |
| A | ASN152 |
| A | TYR222 |
| A | GLY314 |
| A | SER315 |
| A | THR316 |
| A | SER317 |
| A | ARG340 |
| A | HOH569 |
| A | HOH571 |
| site_id | AC3 |
| Number of Residues | 10 |
| Details | binding site for residue ZXM C 401 |
| Chain | Residue |
| C | SER64 |
| C | GLN120 |
| C | TYR150 |
| C | ASN152 |
| C | GLY314 |
| C | SER315 |
| C | THR316 |
| C | SER317 |
| C | ARG340 |
| C | HOH628 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | binding site for residue PO4 C 402 |
| Chain | Residue |
| C | LYS38 |
| C | SER233 |
| C | HIS236 |
| C | TYR244 |
| site_id | AC5 |
| Number of Residues | 11 |
| Details | binding site for residue ZXM D 401 |
| Chain | Residue |
| D | SER64 |
| D | GLN120 |
| D | TYR150 |
| D | ASN152 |
| D | GLY314 |
| D | SER315 |
| D | THR316 |
| D | ARG340 |
| D | ASN343 |
| D | HOH604 |
| D | HOH605 |
Functional Information from PROSITE/UniProt
| site_id | PS00336 |
| Number of Residues | 8 |
| Details | BETA_LACTAMASE_C Beta-lactamase class-C active site. FELGSVSK |
| Chain | Residue | Details |
| B | PHE60-LYS67 |
