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 | 2 |
Details | binding site for residue CL A 301 |
Chain | Residue |
A | ARG206 |
C | ARG206 |
site_id | AC2 |
Number of Residues | 5 |
Details | binding site for residue EDO A 302 |
Chain | Residue |
A | LYS94 |
A | TRP95 |
A | ASP96 |
A | HOH452 |
A | HOH462 |
site_id | AC3 |
Number of Residues | 7 |
Details | binding site for residue EDO A 303 |
Chain | Residue |
A | HOH426 |
A | HOH428 |
A | HOH522 |
C | ASP88 |
C | HIS90 |
A | HIS178 |
A | ASN179 |
site_id | AC4 |
Number of Residues | 5 |
Details | binding site for residue EDO A 304 |
Chain | Residue |
A | GLN64 |
A | ALA65 |
A | PRO217 |
A | HOH483 |
A | HOH554 |
site_id | AC5 |
Number of Residues | 5 |
Details | binding site for residue EDO B 301 |
Chain | Residue |
A | ARG214 |
B | ARG100 |
B | HOH416 |
B | HOH471 |
B | HOH549 |
site_id | AC6 |
Number of Residues | 4 |
Details | binding site for residue EDO B 302 |
Chain | Residue |
B | ASN110 |
B | HOH403 |
B | HOH526 |
B | HOH538 |
site_id | AC7 |
Number of Residues | 7 |
Details | binding site for residue V7V C 301 |
Chain | Residue |
C | SER70 |
C | SER118 |
C | THR209 |
C | GLY210 |
C | TYR211 |
C | ARG250 |
C | HOH401 |
site_id | AC8 |
Number of Residues | 7 |
Details | binding site for residue EDO C 302 |
Chain | Residue |
A | HIS90 |
A | HOH412 |
C | TYR177 |
C | GLU227 |
C | VAL232 |
C | HOH423 |
C | HOH482 |
site_id | AC9 |
Number of Residues | 4 |
Details | binding site for residue EDO C 303 |
Chain | Residue |
B | LYS60 |
B | GLN64 |
C | ASN146 |
C | GLU147 |
site_id | AD1 |
Number of Residues | 9 |
Details | binding site for residue V7V D 301 |
Chain | Residue |
D | SER70 |
D | SER118 |
D | THR209 |
D | GLY210 |
D | TYR211 |
D | SER244 |
D | LEU247 |
D | ARG250 |
D | HOH401 |
site_id | AD2 |
Number of Residues | 1 |
Details | binding site for residue CL D 302 |
site_id | AD3 |
Number of Residues | 4 |
Details | binding site for residue EDO D 303 |
Chain | Residue |
D | LYS94 |
D | TRP95 |
D | ASP96 |
D | HOH432 |
site_id | AD4 |
Number of Residues | 9 |
Details | binding site for residue EDO D 304 |
Chain | Residue |
D | MET115 |
D | ALA194 |
D | MET195 |
D | LEU196 |
D | THR197 |
D | ALA207 |
D | LYS208 |
D | HOH415 |
D | HOH425 |
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 | |