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 | 8 |
Details | binding site for residue GA6 A 301 |
Chain | Residue |
A | SER70 |
A | SER118 |
A | THR209 |
A | GLY210 |
A | TYR211 |
A | SER244 |
A | ARG250 |
A | HOH401 |
site_id | AC2 |
Number of Residues | 5 |
Details | binding site for residue EDO A 302 |
Chain | Residue |
A | THR167 |
A | ILE170 |
A | SER171 |
A | ARG174 |
A | TRP25 |
site_id | AC3 |
Number of Residues | 7 |
Details | binding site for residue EDO A 303 |
Chain | Residue |
A | LYS94 |
A | TRP95 |
A | ASP96 |
A | PRO121 |
A | VAL122 |
A | HOH485 |
A | HOH560 |
site_id | AC4 |
Number of Residues | 7 |
Details | binding site for residue EDO A 304 |
Chain | Residue |
A | TYR177 |
A | GLU227 |
A | VAL232 |
A | HOH412 |
A | HOH419 |
C | HIS90 |
C | HOH498 |
site_id | AC5 |
Number of Residues | 1 |
Details | binding site for residue CL B 301 |
site_id | AC6 |
Number of Residues | 7 |
Details | binding site for residue GA6 B 302 |
Chain | Residue |
B | SER70 |
B | SER118 |
B | THR209 |
B | GLY210 |
B | TYR211 |
B | SER244 |
B | ARG250 |
site_id | AC7 |
Number of Residues | 5 |
Details | binding site for residue EDO B 303 |
Chain | Residue |
B | TYR177 |
B | GLU227 |
B | VAL232 |
B | HOH431 |
B | HOH445 |
site_id | AC8 |
Number of Residues | 7 |
Details | binding site for residue EDO B 304 |
Chain | Residue |
B | LYS39 |
B | SER40 |
B | ASP240 |
B | PRO242 |
B | HOH401 |
B | HOH417 |
B | HOH443 |
site_id | AC9 |
Number of Residues | 2 |
Details | binding site for residue EDO B 305 |
Chain | Residue |
B | ASN110 |
B | HOH574 |
site_id | AD1 |
Number of Residues | 4 |
Details | binding site for residue CL C 301 |
Chain | Residue |
A | ARG206 |
A | HOH647 |
C | ARG206 |
C | HOH607 |
site_id | AD2 |
Number of Residues | 10 |
Details | binding site for residue GA6 C 302 |
Chain | Residue |
C | SER70 |
C | ILE102 |
C | SER118 |
C | THR209 |
C | GLY210 |
C | TYR211 |
C | SER244 |
C | ARG250 |
C | HOH401 |
C | HOH410 |
site_id | AD3 |
Number of Residues | 4 |
Details | binding site for residue EDO C 303 |
Chain | Residue |
C | ILE170 |
C | SER171 |
C | ARG174 |
C | HOH479 |
site_id | AD4 |
Number of Residues | 7 |
Details | binding site for residue EDO C 304 |
Chain | Residue |
A | HIS90 |
A | HOH434 |
C | TYR177 |
C | GLU227 |
C | VAL232 |
C | HOH418 |
C | HOH500 |
site_id | AD5 |
Number of Residues | 4 |
Details | binding site for residue EDO C 305 |
Chain | Residue |
C | PHE93 |
C | LYS94 |
C | TRP95 |
C | ASP96 |
site_id | AD6 |
Number of Residues | 4 |
Details | binding site for residue EDO D 301 |
Chain | Residue |
D | TYR177 |
D | GLU227 |
D | VAL232 |
D | HOH452 |
site_id | AD7 |
Number of Residues | 5 |
Details | binding site for residue EDO D 302 |
Chain | Residue |
D | LYS94 |
D | TRP95 |
D | ASP96 |
D | HOH406 |
D | HOH448 |
site_id | AD8 |
Number of Residues | 5 |
Details | binding site for residue EDO D 303 |
Chain | Residue |
D | TRP47 |
D | ILE170 |
D | SER171 |
D | ARG174 |
D | HOH583 |
site_id | AD9 |
Number of Residues | 11 |
Details | binding site for residue GA6 D 304 |
Chain | Residue |
D | ARG250 |
D | HOH407 |
D | HOH410 |
D | HOH581 |
D | SER70 |
D | ILE102 |
D | SER118 |
D | THR209 |
D | GLY210 |
D | TYR211 |
D | SER244 |
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 | |