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 |
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 |
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 |
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 |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 7 |
Details | binding site for residue QKU A 301 |
Chain | Residue |
A | ILE102 |
A | THR209 |
A | TYR211 |
A | ARG250 |
A | HOH401 |
A | HOH406 |
A | HOH480 |
site_id | AC2 |
Number of Residues | 4 |
Details | binding site for residue CL A 302 |
Chain | Residue |
C | ARG206 |
C | HOH625 |
A | ARG206 |
A | HOH657 |
site_id | AC3 |
Number of Residues | 7 |
Details | binding site for residue EDO A 303 |
Chain | Residue |
A | HIS90 |
A | HOH442 |
A | HOH450 |
A | HOH504 |
C | TYR177 |
C | GLU227 |
C | VAL232 |
site_id | AC4 |
Number of Residues | 6 |
Details | binding site for residue QKU B 301 |
Chain | Residue |
B | ASP101 |
B | THR209 |
B | ARG250 |
B | HOH405 |
B | HOH413 |
B | HOH612 |
site_id | AC5 |
Number of Residues | 2 |
Details | binding site for residue CL B 302 |
Chain | Residue |
B | ARG206 |
B | HOH627 |
site_id | AC6 |
Number of Residues | 6 |
Details | binding site for residue EDO B 303 |
Chain | Residue |
B | TRP25 |
B | TRP47 |
B | SER171 |
B | ARG174 |
B | HOH402 |
B | HOH527 |
site_id | AC7 |
Number of Residues | 5 |
Details | binding site for residue EDO B 304 |
Chain | Residue |
B | ALA65 |
B | PHE66 |
B | PRO217 |
B | HOH428 |
B | HOH576 |
site_id | AC8 |
Number of Residues | 5 |
Details | binding site for residue EDO B 305 |
Chain | Residue |
B | LYS94 |
B | TRP95 |
B | ASP96 |
B | VAL122 |
B | HOH489 |
site_id | AC9 |
Number of Residues | 5 |
Details | binding site for residue EDO B 306 |
Chain | Residue |
B | TYR177 |
B | GLU227 |
B | VAL232 |
B | HOH425 |
B | HOH434 |
site_id | AD1 |
Number of Residues | 6 |
Details | binding site for residue QKU C 301 |
Chain | Residue |
C | ILE102 |
C | THR209 |
C | ARG250 |
C | HOH451 |
C | HOH564 |
C | HOH650 |
site_id | AD2 |
Number of Residues | 5 |
Details | binding site for residue EDO C 302 |
Chain | Residue |
C | TRP25 |
C | THR167 |
C | SER171 |
C | ARG174 |
C | HOH402 |
site_id | AD3 |
Number of Residues | 4 |
Details | binding site for residue EDO D 301 |
Chain | Residue |
D | TRP25 |
D | TRP47 |
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 | |