Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005576 | cellular_component | extracellular region |
A | 0005886 | cellular_component | plasma membrane |
A | 0008800 | molecular_function | beta-lactamase activity |
A | 0016787 | molecular_function | hydrolase activity |
A | 0017001 | biological_process | antibiotic catabolic process |
A | 0030655 | biological_process | beta-lactam antibiotic catabolic process |
A | 0033250 | molecular_function | penicillinase activity |
A | 0033251 | molecular_function | cephalosporinase activity |
A | 0042597 | cellular_component | periplasmic space |
A | 0046677 | biological_process | response to antibiotic |
B | 0005576 | cellular_component | extracellular region |
B | 0005886 | cellular_component | plasma membrane |
B | 0008800 | molecular_function | beta-lactamase activity |
B | 0016787 | molecular_function | hydrolase activity |
B | 0017001 | biological_process | antibiotic catabolic process |
B | 0030655 | biological_process | beta-lactam antibiotic catabolic process |
B | 0033250 | molecular_function | penicillinase activity |
B | 0033251 | molecular_function | cephalosporinase activity |
B | 0042597 | cellular_component | periplasmic space |
B | 0046677 | biological_process | response to antibiotic |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 7 |
Details | binding site for residue PO4 A 401 |
Chain | Residue |
A | SER70 |
A | SER128 |
A | LYS236 |
A | THR237 |
A | GLY238 |
A | THR239 |
A | HOH578 |
site_id | AC2 |
Number of Residues | 4 |
Details | binding site for residue ACT A 402 |
Chain | Residue |
A | LYS205 |
A | HOH594 |
A | PRO202 |
A | ASP204 |
site_id | AC3 |
Number of Residues | 5 |
Details | binding site for residue ACT A 403 |
Chain | Residue |
A | GLY118 |
A | GLN119 |
A | ASP122 |
A | TRP212 |
A | HOH634 |
site_id | AC4 |
Number of Residues | 3 |
Details | binding site for residue ACT A 404 |
Chain | Residue |
A | ARG173 |
A | ASP241 |
A | TYR273 |
site_id | AC5 |
Number of Residues | 6 |
Details | binding site for residue PO4 B 401 |
Chain | Residue |
B | SER70 |
B | SER128 |
B | LYS236 |
B | THR237 |
B | GLY238 |
B | THR239 |
site_id | AC6 |
Number of Residues | 4 |
Details | binding site for residue PO4 B 402 |
Chain | Residue |
A | HIS300 |
B | ARG173 |
B | ASP241 |
B | TYR273 |
site_id | AC7 |
Number of Residues | 4 |
Details | binding site for residue ACT B 403 |
Chain | Residue |
B | PRO202 |
B | ASP204 |
B | LYS205 |
B | HOH608 |
site_id | AC8 |
Number of Residues | 5 |
Details | binding site for residue ETE B 404 |
Chain | Residue |
A | HOH612 |
B | THR210 |
B | ALA214 |
B | LYS232 |
B | TRP252 |
site_id | AC9 |
Number of Residues | 7 |
Details | binding site for residue AE4 B 405 |
Chain | Residue |
B | ALA31 |
B | ALA57 |
B | ILE58 |
B | GLU59 |
B | TYR60 |
B | ARG61 |
B | HOH509 |
Functional Information from PROSITE/UniProt
site_id | PS00146 |
Number of Residues | 16 |
Details | BETA_LACTAMASE_A Beta-lactamase class-A active site. FaFCSTfKaplVAAVL |
Chain | Residue | Details |
A | PHE66-LEU81 | |
Functional Information from SwissProt/UniProt
Chain | Residue | Details |
A | SER70 | |
B | SER70 | |
Chain | Residue | Details |
A | GLU168 | |
B | GLU168 | |
Chain | Residue | Details |
A | SER128 | |
A | THR237 | |
B | SER128 | |
B | THR237 | |
Chain | Residue | Details |
A | LYS73 | |
B | LYS73 | |
site_id | SWS_FT_FI5 |
Number of Residues | 2 |
Details | SITE: Functions as a gatekeeper residue that regulates substrate accessibility to the enzyme active site => ECO:0000303|PubMed:24023821 |
Chain | Residue | Details |
A | ILE103 | |
B | ILE103 | |