Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0008658 | molecular_function | penicillin binding |
A | 0008800 | molecular_function | beta-lactamase activity |
A | 0016787 | molecular_function | hydrolase activity |
A | 0017001 | biological_process | antibiotic catabolic process |
A | 0046677 | biological_process | response to antibiotic |
B | 0008658 | molecular_function | penicillin binding |
B | 0008800 | molecular_function | beta-lactamase activity |
B | 0016787 | molecular_function | hydrolase activity |
B | 0017001 | biological_process | antibiotic catabolic process |
B | 0046677 | biological_process | response to antibiotic |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 11 |
Details | binding site for residue 5R7 A 301 |
Chain | Residue |
A | GLN100 |
A | HOH469 |
A | HOH485 |
A | SER101 |
A | TRP136 |
A | SER149 |
A | VAL151 |
A | GLY241 |
A | SER242 |
A | THR269 |
A | HOH439 |
site_id | AC2 |
Number of Residues | 8 |
Details | binding site for residue FLC A 302 |
Chain | Residue |
A | HIS168 |
A | ALA172 |
A | HIS285 |
A | HOH414 |
A | HOH441 |
A | HOH495 |
A | HOH520 |
A | HOH539 |
site_id | AC3 |
Number of Residues | 15 |
Details | binding site for Di-peptide 5R7 B 300 and SER B 101 |
Chain | Residue |
B | PRO99 |
B | GLN100 |
B | THR102 |
B | PHE103 |
B | LYS104 |
B | GLU132 |
B | TRP136 |
B | SER149 |
B | VAL151 |
B | LEU189 |
B | LYS239 |
B | THR240 |
B | GLY241 |
B | SER242 |
B | HOH404 |
Functional Information from PROSITE/UniProt
site_id | PS00337 |
Number of Residues | 11 |
Details | BETA_LACTAMASE_D Beta-lactamase class-D active site. PqSTFKVAnAL |
Chain | Residue | Details |
A | PRO99-LEU109 | |