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 | 5 |
Details | binding site for residue XEV A 301 |
Chain | Residue |
A | TYR117 |
A | TYR211 |
A | ARG250 |
A | HOH405 |
A | HOH451 |
site_id | AC2 |
Number of Residues | 3 |
Details | binding site for residue XEV B 301 |
Chain | Residue |
B | THR209 |
B | ARG250 |
B | HOH415 |
site_id | AC3 |
Number of Residues | 3 |
Details | binding site for residue EDO B 302 |
Chain | Residue |
B | ASP96 |
B | HOH418 |
B | LYS94 |
site_id | AC4 |
Number of Residues | 1 |
Details | binding site for residue EDO B 303 |
site_id | AC5 |
Number of Residues | 4 |
Details | binding site for residue EDO C 301 |
Chain | Residue |
C | THR167 |
C | ILE170 |
C | SER171 |
C | ARG174 |
site_id | AC6 |
Number of Residues | 3 |
Details | binding site for residue XEV D 301 |
Chain | Residue |
D | TYR117 |
D | THR209 |
D | ARG250 |
site_id | AC7 |
Number of Residues | 1 |
Details | binding site for residue CL D 302 |
site_id | AC8 |
Number of Residues | 3 |
Details | binding site for residue EDO D 303 |
Chain | Residue |
D | GLU227 |
D | ASP229 |
D | HOH466 |
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 | |