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 | 4 |
| Details | binding site for residue ZN A 300 |
| Chain | Residue |
| A | HIS120 |
| A | HIS122 |
| A | HIS189 |
| A | HOH432 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | binding site for residue ZN A 301 |
| Chain | Residue |
| B | HOH412 |
| A | ASP124 |
| A | CYS208 |
| A | HIS250 |
| A | FMT306 |
| A | HOH432 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | binding site for residue ZN A 302 |
| Chain | Residue |
| A | GLU152 |
| A | ASP223 |
| A | FMT303 |
| B | GLU227 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | binding site for residue FMT A 303 |
| Chain | Residue |
| A | HIS122 |
| A | GLU152 |
| A | ASP223 |
| A | ZN302 |
| A | HOH494 |
| B | GLU227 |
| site_id | AC5 |
| Number of Residues | 1 |
| Details | binding site for residue FMT A 304 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | binding site for residue FMT A 305 |
| Chain | Residue |
| A | PRO112 |
| A | VAL113 |
| A | HOH413 |
| A | HOH499 |
| site_id | AC7 |
| Number of Residues | 8 |
| Details | binding site for residue FMT A 306 |
| Chain | Residue |
| A | HIS189 |
| A | CYS208 |
| A | LYS211 |
| A | GLY219 |
| A | ASN220 |
| A | HIS250 |
| A | ZN301 |
| B | GLY69 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | binding site for residue ZN B 300 |
| Chain | Residue |
| B | HIS120 |
| B | HIS122 |
| B | HIS189 |
| B | ZN301 |
| B | HOH420 |
| B | HOH454 |
| site_id | AC9 |
| Number of Residues | 6 |
| Details | binding site for residue ZN B 301 |
| Chain | Residue |
| B | ASP124 |
| B | CYS208 |
| B | HIS250 |
| B | ZN300 |
| B | FMT305 |
| B | HOH420 |
| site_id | AD1 |
| Number of Residues | 4 |
| Details | binding site for residue ZN B 302 |
| Chain | Residue |
| A | GLU227 |
| B | GLU152 |
| B | ASP223 |
| B | FMT303 |
| site_id | AD2 |
| Number of Residues | 4 |
| Details | binding site for residue FMT B 303 |
| Chain | Residue |
| A | GLU227 |
| B | GLU152 |
| B | ASP223 |
| B | ZN302 |
| site_id | AD3 |
| Number of Residues | 5 |
| Details | binding site for residue MG B 304 |
| Chain | Residue |
| B | ASP95 |
| B | ASP130 |
| B | HOH418 |
| B | HOH487 |
| B | HOH492 |
| site_id | AD4 |
| Number of Residues | 7 |
| Details | binding site for residue FMT B 305 |
| Chain | Residue |
| B | HIS189 |
| B | CYS208 |
| B | LYS211 |
| B | GLY219 |
| B | ASN220 |
| B | HIS250 |
| B | ZN301 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI2 |
| Number of Residues | 12 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"22713171","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"25815530","evidenceCode":"ECO:0000269"}]} |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"22713171","evidenceCode":"ECO:0000269"}]} |
