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 | 10 |
Details | binding site for residue IQQ A 301 |
Chain | Residue |
A | ILE102 |
A | HOH710 |
A | TYR117 |
A | THR209 |
A | TYR211 |
A | SER244 |
A | ARG250 |
A | HOH412 |
A | HOH592 |
A | HOH700 |
site_id | AC2 |
Number of Residues | 6 |
Details | binding site for residue EDO A 302 |
Chain | Residue |
A | SER40 |
A | ASP240 |
A | MET241 |
A | PRO242 |
A | HOH433 |
A | HOH475 |
site_id | AC3 |
Number of Residues | 2 |
Details | binding site for residue EDO A 303 |
Chain | Residue |
A | HIS38 |
A | GLU256 |
site_id | AC4 |
Number of Residues | 5 |
Details | binding site for residue EDO A 304 |
Chain | Residue |
A | LEU81 |
A | SER184 |
A | ARG186 |
A | SER187 |
A | HOH496 |
site_id | AC5 |
Number of Residues | 3 |
Details | binding site for residue CL A 305 |
Chain | Residue |
A | ARG206 |
C | ARG206 |
C | HOH630 |
site_id | AC6 |
Number of Residues | 7 |
Details | binding site for residue IQQ B 301 |
Chain | Residue |
B | ILE102 |
B | TYR117 |
B | THR209 |
B | SER244 |
B | ARG250 |
B | HOH403 |
B | HOH684 |
site_id | AC7 |
Number of Residues | 7 |
Details | binding site for residue EDO B 302 |
Chain | Residue |
B | LYS39 |
B | SER40 |
B | ASP240 |
B | MET241 |
B | PRO242 |
B | HOH444 |
B | HOH462 |
site_id | AC8 |
Number of Residues | 5 |
Details | binding site for residue EDO B 303 |
Chain | Residue |
B | SER184 |
B | ARG186 |
B | SER187 |
B | HOH470 |
B | HOH516 |
site_id | AC9 |
Number of Residues | 1 |
Details | binding site for residue CL B 304 |
site_id | AD1 |
Number of Residues | 7 |
Details | binding site for residue IQQ C 301 |
Chain | Residue |
C | ILE102 |
C | TYR117 |
C | THR209 |
C | SER244 |
C | ARG250 |
C | HOH401 |
C | HOH417 |
site_id | AD2 |
Number of Residues | 5 |
Details | binding site for residue EDO C 302 |
Chain | Residue |
C | LEU81 |
C | SER184 |
C | ARG186 |
C | SER187 |
C | HOH462 |
site_id | AD3 |
Number of Residues | 4 |
Details | binding site for residue EDO C 303 |
Chain | Residue |
C | VAL85 |
C | GLN91 |
C | GLN129 |
C | HOH592 |
site_id | AD4 |
Number of Residues | 8 |
Details | binding site for residue IQQ D 301 |
Chain | Residue |
D | ILE102 |
D | TYR117 |
D | TYR211 |
D | SER244 |
D | ARG250 |
D | HOH401 |
D | HOH412 |
D | HOH417 |
site_id | AD5 |
Number of Residues | 5 |
Details | binding site for residue EDO D 302 |
Chain | Residue |
D | LEU81 |
D | SER184 |
D | ARG186 |
D | SER187 |
D | HOH444 |
site_id | AD6 |
Number of Residues | 3 |
Details | binding site for residue EDO D 303 |
Chain | Residue |
D | THR167 |
D | SER171 |
D | ARG174 |
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 | |