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 |
A | 0046872 | molecular_function | metal ion binding |
A | 0071555 | biological_process | cell wall organization |
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 |
B | 0046872 | molecular_function | metal ion binding |
B | 0071555 | biological_process | cell wall organization |
C | 0008658 | molecular_function | penicillin binding |
C | 0008800 | molecular_function | beta-lactamase activity |
C | 0016787 | molecular_function | hydrolase activity |
C | 0017001 | biological_process | antibiotic catabolic process |
C | 0046677 | biological_process | response to antibiotic |
C | 0046872 | molecular_function | metal ion binding |
C | 0071555 | biological_process | cell wall organization |
D | 0008658 | molecular_function | penicillin binding |
D | 0008800 | molecular_function | beta-lactamase activity |
D | 0016787 | molecular_function | hydrolase activity |
D | 0017001 | biological_process | antibiotic catabolic process |
D | 0046677 | biological_process | response to antibiotic |
D | 0046872 | molecular_function | metal ion binding |
D | 0071555 | biological_process | cell wall organization |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 8 |
Details | binding site for residue Q2S A 301 |
Chain | Residue |
A | THR209 |
A | SER244 |
A | ARG250 |
A | HOH422 |
A | HOH428 |
A | HOH550 |
A | HOH559 |
A | HOH726 |
site_id | AC2 |
Number of Residues | 6 |
Details | binding site for residue Q2S B 301 |
Chain | Residue |
B | ARG250 |
B | HOH401 |
B | HOH494 |
B | HOH524 |
B | HOH538 |
B | SER244 |
site_id | AC3 |
Number of Residues | 2 |
Details | binding site for residue CL B 302 |
Chain | Residue |
B | ARG206 |
B | HOH546 |
site_id | AC4 |
Number of Residues | 3 |
Details | binding site for residue Q2S C 301 |
Chain | Residue |
C | THR209 |
C | SER244 |
C | ARG250 |
site_id | AC5 |
Number of Residues | 3 |
Details | binding site for residue CL C 302 |
Chain | Residue |
A | ARG206 |
A | HOH606 |
C | ARG206 |
site_id | AC6 |
Number of Residues | 6 |
Details | binding site for residue EDO C 303 |
Chain | Residue |
C | LEU196 |
C | THR197 |
C | ALA207 |
C | LYS208 |
C | THR209 |
C | HOH463 |
site_id | AC7 |
Number of Residues | 10 |
Details | binding site for residue Q2S D 301 |
Chain | Residue |
D | ILE102 |
D | SER118 |
D | THR209 |
D | GLY210 |
D | SER244 |
D | ARG250 |
D | HOH427 |
D | HOH475 |
D | HOH480 |
D | HOH492 |
Functional Information from PROSITE/UniProt
site_id | PS00337 |
Number of Residues | 11 |
Details | BETA_LACTAMASE_D Beta-lactamase class-D active site. PaSTFKIPnSL |
Chain | Residue | Details |
A | PRO68-LEU78 | |