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 |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 9 |
Details | binding site for residue GOL A 301 |
Chain | Residue |
A | GLN83 |
A | ASN86 |
A | ASP141 |
A | ASP240 |
A | TYR272 |
A | ASP273 |
A | GOL302 |
A | HOH404 |
A | HOH441 |
site_id | AC2 |
Number of Residues | 10 |
Details | binding site for residue GOL A 302 |
Chain | Residue |
A | ALA140 |
A | ASP141 |
A | GLU275 |
A | PRO276 |
A | GOL301 |
A | HOH404 |
A | HOH464 |
A | HOH474 |
A | HOH482 |
A | HOH595 |
site_id | AC3 |
Number of Residues | 9 |
Details | binding site for residue GOL A 303 |
Chain | Residue |
A | PRO107 |
A | GLN110 |
A | GLN111 |
A | THR145 |
A | ALA146 |
A | THR149 |
A | ARG161 |
A | LEU162 |
A | ASP163 |
site_id | AC4 |
Number of Residues | 10 |
Details | binding site for residue GOL A 304 |
Chain | Residue |
A | TYR97 |
A | VAL113 |
A | VAL291 |
A | LEU292 |
A | ALA293 |
A | HOH406 |
A | HOH412 |
A | HOH593 |
A | HOH603 |
A | HOH615 |
site_id | AC5 |
Number of Residues | 11 |
Details | binding site for residue GOL A 305 |
Chain | Residue |
A | MET211 |
A | ALA212 |
A | GLY217 |
A | ALA218 |
A | ARG222 |
A | VAL231 |
A | ILE232 |
A | ASP233 |
A | HOH413 |
A | HOH419 |
A | HOH478 |
site_id | AC6 |
Number of Residues | 6 |
Details | binding site for residue GOL A 306 |
Chain | Residue |
A | THR89 |
A | HIS90 |
A | LYS93 |
A | ASP273 |
A | HOH411 |
A | HOH473 |
site_id | AC7 |
Number of Residues | 8 |
Details | binding site for residue GOL A 307 |
Chain | Residue |
A | ALA30 |
A | ALA56 |
A | ILE57 |
A | GLU59 |
A | TYR60 |
A | HOH409 |
A | HOH461 |
A | HOH467 |
site_id | AC8 |
Number of Residues | 8 |
Details | binding site for residue GOL A 308 |
Chain | Residue |
A | ARG65 |
A | PRO174 |
A | GLY175 |
A | ARG243 |
A | HOH468 |
A | HOH524 |
A | HOH639 |
A | HOH642 |
site_id | AC9 |
Number of Residues | 4 |
Details | binding site for residue EDO A 309 |
Chain | Residue |
A | ASP101 |
A | ASN136 |
A | GLU165 |
A | HOH484 |
site_id | AD1 |
Number of Residues | 10 |
Details | binding site for residue PO4 A 310 |
Chain | Residue |
A | SER70 |
A | SER130 |
A | LYS234 |
A | THR235 |
A | GLY236 |
A | THR237 |
A | HOH401 |
A | HOH462 |
A | HOH630 |
A | HOH645 |
site_id | AD2 |
Number of Residues | 3 |
Details | binding site for residue PO4 A 311 |
Chain | Residue |
A | LEU94 |
A | GLY116 |
A | GLN121 |
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 | |
Chain | Residue | Details |
A | GLU166 | |
Chain | Residue | Details |
A | SER130 | |
A | THR235 | |
Chain | Residue | Details |
A | LYS73 | |
site_id | SWS_FT_FI5 |
Number of Residues | 1 |
Details | SITE: Functions as a gatekeeper residue that regulates substrate accessibility to the enzyme active site => ECO:0000303|PubMed:24023821 |
Chain | Residue | Details |
A | ILE105 | |