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 | 2 |
Details | binding site for residue CL A 301 |
Chain | Residue |
A | ARG206 |
D | ARG206 |
site_id | AC2 |
Number of Residues | 5 |
Details | binding site for residue EDO A 302 |
Chain | Residue |
A | LEU81 |
A | SER184 |
A | ARG186 |
A | SER187 |
A | HOH404 |
site_id | AC3 |
Number of Residues | 7 |
Details | binding site for residue EDO A 303 |
Chain | Residue |
A | VAL232 |
A | HOH406 |
D | HIS90 |
D | GLN193 |
D | HOH440 |
A | TYR177 |
A | GLU227 |
site_id | AC4 |
Number of Residues | 9 |
Details | binding site for residue F1C B 301 |
Chain | Residue |
B | SER70 |
B | VAL120 |
B | THR209 |
B | THR213 |
B | ARG214 |
B | SER244 |
B | LEU247 |
B | ARG250 |
B | HOH437 |
site_id | AC5 |
Number of Residues | 1 |
Details | binding site for residue CL B 302 |
site_id | AC6 |
Number of Residues | 1 |
Details | binding site for residue EDO B 303 |
site_id | AC7 |
Number of Residues | 5 |
Details | binding site for residue EDO B 304 |
Chain | Residue |
B | TYR177 |
B | GLU227 |
B | VAL232 |
B | HOH418 |
B | HOH426 |
site_id | AC8 |
Number of Residues | 2 |
Details | binding site for residue EDO B 305 |
Chain | Residue |
B | ARG107 |
B | ASN110 |
site_id | AC9 |
Number of Residues | 3 |
Details | binding site for residue EDO C 301 |
Chain | Residue |
C | LYS116 |
C | HOH407 |
C | HOH434 |
site_id | AD1 |
Number of Residues | 3 |
Details | binding site for residue EDO C 302 |
Chain | Residue |
C | SER171 |
C | ARG174 |
C | HOH437 |
site_id | AD2 |
Number of Residues | 9 |
Details | binding site for residue F1C D 301 |
Chain | Residue |
D | SER70 |
D | VAL120 |
D | THR209 |
D | TYR211 |
D | ARG214 |
D | SER244 |
D | LEU247 |
D | ARG250 |
D | HOH401 |
site_id | AD3 |
Number of Residues | 5 |
Details | binding site for residue EDO D 302 |
Chain | Residue |
A | ASN200 |
A | ASP229 |
D | LYS116 |
D | HOH418 |
D | HOH441 |
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 | |