Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0008658 | molecular_function | penicillin binding |
A | 0008800 | molecular_function | beta-lactamase activity |
A | 0017001 | biological_process | antibiotic catabolic process |
B | 0008658 | molecular_function | penicillin binding |
B | 0008800 | molecular_function | beta-lactamase activity |
B | 0017001 | biological_process | antibiotic catabolic process |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 17 |
Details | binding site for residue 1RG A 301 |
Chain | Residue |
A | ALA66 |
A | LYS251 |
A | MG303 |
A | HOH406 |
A | HOH439 |
A | HOH441 |
A | HOH460 |
A | HOH484 |
A | HOH562 |
A | SER67 |
A | SER115 |
A | VAL117 |
A | THR206 |
A | GLY207 |
A | PHE208 |
A | GLU244 |
A | ARG250 |
site_id | AC2 |
Number of Residues | 3 |
Details | binding site for residue FMT A 302 |
Chain | Residue |
A | PRO217 |
A | HOH403 |
A | HOH478 |
site_id | AC3 |
Number of Residues | 6 |
Details | binding site for residue MG A 303 |
Chain | Residue |
A | ALA66 |
A | SER67 |
A | KCX70 |
A | LEU155 |
A | 1RG301 |
A | HOH607 |
site_id | AC4 |
Number of Residues | 4 |
Details | binding site for residue MG A 304 |
Chain | Residue |
A | GLN122 |
A | ASP242 |
A | HOH476 |
A | HOH672 |
site_id | AC5 |
Number of Residues | 4 |
Details | binding site for residue FMT B 302 |
Chain | Residue |
A | LYS61 |
A | HOH401 |
B | GLU62 |
B | HOH417 |
site_id | AC6 |
Number of Residues | 18 |
Details | binding site for Di-peptide 1RG B 301 and SER B 67 |
Chain | Residue |
B | PRO65 |
B | ALA66 |
B | THR68 |
B | PHE69 |
B | KCX70 |
B | MET99 |
B | SER115 |
B | VAL117 |
B | LYS205 |
B | THR206 |
B | GLY207 |
B | PHE208 |
B | LEU247 |
B | ARG250 |
B | LYS251 |
B | HOH408 |
B | HOH441 |
B | HOH446 |
Functional Information from PROSITE/UniProt
site_id | PS00337 |
Number of Residues | 11 |
Details | BETA_LACTAMASE_D Beta-lactamase class-D active site. PaSTFKIPnAI |
Chain | Residue | Details |
A | PRO65-ILE75 | |