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 | 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 | 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 | 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 | 0071555 | biological_process | cell wall organization |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 6 |
Details | binding site for residue GOL A 301 |
Chain | Residue |
A | SER60 |
A | LYS63 |
A | ASP108 |
A | LYS206 |
A | GLY208 |
A | THR209 |
site_id | AC2 |
Number of Residues | 8 |
Details | binding site for residue PO4 B 300 |
Chain | Residue |
D | ASP196 |
D | ALA197 |
D | PRO198 |
D | GLU199 |
D | SER200 |
B | ARG93 |
B | TYR211 |
B | EDO302 |
site_id | AC3 |
Number of Residues | 6 |
Details | binding site for residue EDO B 301 |
Chain | Residue |
B | LYS80 |
B | THR81 |
B | PRO82 |
B | ALA83 |
B | HOH407 |
C | ARG97 |
site_id | AC4 |
Number of Residues | 5 |
Details | binding site for residue EDO B 302 |
Chain | Residue |
B | TYR211 |
B | ARG213 |
B | PRO219 |
B | PO4300 |
D | GLU199 |
site_id | AC5 |
Number of Residues | 8 |
Details | binding site for residue PO4 C 300 |
Chain | Residue |
A | ARG93 |
A | THR209 |
A | TYR211 |
C | ALA197 |
C | PRO198 |
C | GLU199 |
C | SER200 |
C | HOH409 |
site_id | AC6 |
Number of Residues | 4 |
Details | binding site for residue EDO C 301 |
Chain | Residue |
C | ASP85 |
C | LYS87 |
C | THR90 |
C | TRP112 |
site_id | AC7 |
Number of Residues | 5 |
Details | binding site for residue EDO D 301 |
Chain | Residue |
D | ASP85 |
D | LYS87 |
D | THR90 |
D | TRP112 |
D | GLU116 |
Functional Information from PROSITE/UniProt
site_id | PS00337 |
Number of Residues | 11 |
Details | BETA_LACTAMASE_D Beta-lactamase class-D active site. PaSTFKVPlAL |
Chain | Residue | Details |
A | PRO58-LEU68 | |