Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0008270 | molecular_function | zinc ion binding |
| A | 0008800 | molecular_function | beta-lactamase activity |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0017001 | biological_process | antibiotic catabolic process |
| A | 0042597 | cellular_component | periplasmic space |
| A | 0046677 | biological_process | response to antibiotic |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0008270 | molecular_function | zinc ion binding |
| B | 0008800 | molecular_function | beta-lactamase activity |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0017001 | biological_process | antibiotic catabolic process |
| B | 0042597 | cellular_component | periplasmic space |
| B | 0046677 | biological_process | response to antibiotic |
| B | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | binding site for residue ZN A 301 |
| Chain | Residue |
| A | HIS120 |
| A | HIS122 |
| A | HIS189 |
| A | HOH412 |
| A | HOH571 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | binding site for residue ZN A 302 |
| Chain | Residue |
| A | HOH588 |
| A | ASP124 |
| A | CYS208 |
| A | HIS250 |
| A | HOH412 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | binding site for residue CA A 303 |
| Chain | Residue |
| A | GLU152 |
| A | ASP223 |
| A | HOH456 |
| A | HOH558 |
| B | GLU227 |
| B | HOH551 |
| site_id | AC4 |
| Number of Residues | 7 |
| Details | binding site for residue CA A 304 |
| Chain | Residue |
| A | ASP95 |
| A | ASP130 |
| A | HOH454 |
| A | HOH569 |
| A | HOH576 |
| A | HOH600 |
| A | HOH603 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | binding site for residue CL A 305 |
| Chain | Residue |
| A | PHE240 |
| A | PRO241 |
| A | LYS242 |
| A | ALA243 |
| A | HOH649 |
| A | HOH657 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | binding site for residue CL A 306 |
| Chain | Residue |
| A | ALA55 |
| A | PRO56 |
| A | ASN57 |
| A | HOH589 |
| A | HOH627 |
| site_id | AC7 |
| Number of Residues | 8 |
| Details | binding site for residue EPE B 301 |
| Chain | Residue |
| A | GLN44 |
| A | GLN107 |
| A | GLU108 |
| A | HOH465 |
| B | ARG234 |
| B | THR260 |
| B | ARG264 |
| B | HOH691 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | binding site for residue ZN B 302 |
| Chain | Residue |
| B | HIS120 |
| B | HIS122 |
| B | HIS189 |
| B | HOH408 |
| B | HOH538 |
| site_id | AC9 |
| Number of Residues | 5 |
| Details | binding site for residue ZN B 303 |
| Chain | Residue |
| B | ASP124 |
| B | CYS208 |
| B | HIS250 |
| B | HOH408 |
| B | HOH599 |
| site_id | AD1 |
| Number of Residues | 6 |
| Details | binding site for residue CA B 304 |
| Chain | Residue |
| A | GLU227 |
| A | HOH535 |
| B | GLU152 |
| B | ASP223 |
| B | HOH580 |
| B | HOH597 |
| site_id | AD2 |
| Number of Residues | 7 |
| Details | binding site for residue CA B 305 |
| Chain | Residue |
| A | HOH510 |
| A | HOH543 |
| B | GLY178 |
| B | HOH496 |
| B | HOH554 |
| B | HOH594 |
| B | HOH638 |
| site_id | AD3 |
| Number of Residues | 5 |
| Details | binding site for residue CA B 306 |
| Chain | Residue |
| B | ASP95 |
| B | ASP130 |
| B | HOH442 |
| B | HOH522 |
| B | HOH620 |
| site_id | AD4 |
| Number of Residues | 5 |
| Details | binding site for residue CL B 307 |
| Chain | Residue |
| A | ARG264 |
| A | HOH554 |
| B | SER160 |
| B | HOH409 |
| B | HOH430 |
| site_id | AD5 |
| Number of Residues | 7 |
| Details | binding site for residue CL B 308 |
| Chain | Residue |
| B | PHE240 |
| B | PRO241 |
| B | LYS242 |
| B | ALA243 |
| B | HOH421 |
| B | HOH634 |
| B | HOH675 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"22713171","evidenceCode":"ECO:0000269"}]} |
