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 |
A | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 12 |
Details | binding site for residue 1S7 A 401 |
Chain | Residue |
A | SER64 |
A | GLY316 |
A | SER317 |
A | HOH708 |
A | LYS67 |
A | LEU119 |
A | GLN120 |
A | PHE150 |
A | ASN152 |
A | ALA221 |
A | TYR222 |
A | PHE292 |
site_id | AC2 |
Number of Residues | 3 |
Details | binding site for residue ZN A 402 |
Chain | Residue |
A | GLU5 |
A | HIS39 |
A | HOH764 |
site_id | AC3 |
Number of Residues | 3 |
Details | binding site for residue ZN A 403 |
Chain | Residue |
A | HIS1 |
A | GLU361 |
A | HOH750 |
site_id | AC4 |
Number of Residues | 3 |
Details | binding site for residue ZN A 404 |
Chain | Residue |
A | GLU124 |
A | ASP126 |
A | HOH786 |
site_id | AC5 |
Number of Residues | 4 |
Details | binding site for residue ZN A 405 |
Chain | Residue |
A | HIS160 |
A | HOH563 |
A | HOH778 |
A | HOH781 |
site_id | AC6 |
Number of Residues | 3 |
Details | binding site for residue ZN A 406 |
Chain | Residue |
A | HIS185 |
A | HOH773 |
A | HOH775 |
site_id | AC7 |
Number of Residues | 3 |
Details | binding site for residue NA A 407 |
Chain | Residue |
A | HIS160 |
A | GLU220 |
A | HOH751 |
site_id | AC8 |
Number of Residues | 5 |
Details | binding site for residue ZN A 408 |
Chain | Residue |
A | HIS255 |
A | GLU308 |
A | HOH501 |
A | HOH761 |
A | HOH787 |
Functional Information from PROSITE/UniProt
site_id | PS00336 |
Number of Residues | 8 |
Details | BETA_LACTAMASE_C Beta-lactamase class-C active site. FEIGSVSK |
Chain | Residue | Details |
A | PHE60-LYS67 | |