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 | 6 |
Details | binding site for residue L5D A 301 |
Chain | Residue |
A | ILE102 |
A | TYR117 |
A | THR209 |
A | SER244 |
A | ARG250 |
A | HOH564 |
site_id | AC2 |
Number of Residues | 6 |
Details | binding site for residue EDO A 302 |
Chain | Residue |
A | PRO242 |
A | HOH426 |
A | HOH432 |
A | SER40 |
A | ASP240 |
A | MET241 |
site_id | AC3 |
Number of Residues | 5 |
Details | binding site for residue EDO A 303 |
Chain | Residue |
A | LYS94 |
A | TRP95 |
A | ASP96 |
A | HOH455 |
A | HOH494 |
site_id | AC4 |
Number of Residues | 7 |
Details | binding site for residue L5D B 301 |
Chain | Residue |
B | TYR117 |
B | SER244 |
B | ARG250 |
B | HOH404 |
B | HOH412 |
B | HOH530 |
B | HOH569 |
site_id | AC5 |
Number of Residues | 6 |
Details | binding site for residue EDO B 302 |
Chain | Residue |
B | LYS94 |
B | TRP95 |
B | ASP96 |
B | HOH415 |
B | HOH424 |
B | HOH545 |
site_id | AC6 |
Number of Residues | 7 |
Details | binding site for residue EDO B 303 |
Chain | Residue |
B | LYS39 |
B | SER40 |
B | MET239 |
B | ASP240 |
B | MET241 |
B | PRO242 |
B | HOH469 |
site_id | AC7 |
Number of Residues | 5 |
Details | binding site for residue EDO B 304 |
Chain | Residue |
B | ALA65 |
B | PHE66 |
B | PRO217 |
B | HOH570 |
C | HOH494 |
site_id | AC8 |
Number of Residues | 9 |
Details | binding site for residue L5D C 301 |
Chain | Residue |
C | ILE102 |
C | TYR117 |
C | SER118 |
C | THR209 |
C | TYR211 |
C | SER244 |
C | ARG250 |
C | HOH435 |
C | HOH543 |
site_id | AC9 |
Number of Residues | 4 |
Details | binding site for residue CL C 302 |
Chain | Residue |
A | ARG206 |
A | HOH617 |
C | ARG206 |
C | HOH594 |
site_id | AD1 |
Number of Residues | 2 |
Details | binding site for residue EDO C 303 |
Chain | Residue |
C | SER171 |
C | ARG174 |
site_id | AD2 |
Number of Residues | 8 |
Details | binding site for residue L5D D 301 |
Chain | Residue |
D | TYR117 |
D | THR209 |
D | TYR211 |
D | SER244 |
D | ARG250 |
D | HOH440 |
D | HOH534 |
D | HOH536 |
site_id | AD3 |
Number of Residues | 5 |
Details | binding site for residue CL D 302 |
Chain | Residue |
D | LEU228 |
D | ASN231 |
D | VAL232 |
D | HOH418 |
D | HOH629 |
site_id | AD4 |
Number of Residues | 1 |
Details | binding site for residue CL D 303 |
site_id | AD5 |
Number of Residues | 4 |
Details | binding site for residue EDO D 304 |
Chain | Residue |
D | TRP25 |
D | LEU59 |
D | ASN63 |
D | THR167 |
site_id | AD6 |
Number of Residues | 2 |
Details | binding site for residue EDO D 305 |
Chain | Residue |
D | ARG100 |
D | ASP101 |
site_id | AD7 |
Number of Residues | 5 |
Details | binding site for residue EDO D 306 |
Chain | Residue |
D | LEU81 |
D | SER184 |
D | ARG186 |
D | SER187 |
D | HOH466 |
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 | |