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 | 3 |
Details | binding site for residue CL A 301 |
Chain | Residue |
A | ARG206 |
A | HOH564 |
B | ARG206 |
site_id | AC2 |
Number of Residues | 2 |
Details | binding site for residue CL A 302 |
Chain | Residue |
A | LYS73 |
A | TRP157 |
site_id | AC3 |
Number of Residues | 16 |
Details | binding site for residue ID1 A 303 |
Chain | Residue |
A | LEU158 |
A | THR209 |
A | GLY210 |
A | TYR211 |
A | SER244 |
A | LEU247 |
A | ARG250 |
A | HOH407 |
A | HOH420 |
A | HOH491 |
A | HOH508 |
A | HOH524 |
A | ALA69 |
A | SER70 |
A | SER118 |
A | VAL120 |
site_id | AC4 |
Number of Residues | 3 |
Details | binding site for residue CL B 301 |
Chain | Residue |
B | LYS73 |
B | TRP157 |
B | HOH547 |
site_id | AC5 |
Number of Residues | 3 |
Details | binding site for residue CL C 301 |
Chain | Residue |
C | ARG206 |
C | HOH530 |
D | ARG206 |
site_id | AC6 |
Number of Residues | 2 |
Details | binding site for residue CL C 302 |
Chain | Residue |
C | LYS73 |
C | TRP157 |
site_id | AC7 |
Number of Residues | 2 |
Details | binding site for residue CL D 301 |
Chain | Residue |
D | LYS73 |
D | TRP157 |
site_id | AC8 |
Number of Residues | 14 |
Details | binding site for Di-peptide ID1 B 302 and SER B 70 |
Chain | Residue |
B | PRO68 |
B | ALA69 |
B | THR71 |
B | PHE72 |
B | LYS73 |
B | SER118 |
B | VAL120 |
B | LEU158 |
B | LYS208 |
B | THR209 |
B | GLY210 |
B | TYR211 |
B | ARG250 |
B | HOH542 |
site_id | AC9 |
Number of Residues | 14 |
Details | binding site for Di-peptide ID1 C 303 and SER C 70 |
Chain | Residue |
C | PRO68 |
C | ALA69 |
C | THR71 |
C | PHE72 |
C | LYS73 |
C | SER118 |
C | VAL120 |
C | LEU158 |
C | LYS208 |
C | THR209 |
C | GLY210 |
C | TYR211 |
C | SER244 |
C | ARG250 |
site_id | AD1 |
Number of Residues | 15 |
Details | binding site for Di-peptide ID1 D 302 and SER D 70 |
Chain | Residue |
D | PRO68 |
D | ALA69 |
D | THR71 |
D | PHE72 |
D | LYS73 |
D | SER118 |
D | VAL120 |
D | LEU158 |
D | LYS208 |
D | THR209 |
D | GLY210 |
D | TYR211 |
D | LEU247 |
D | ARG250 |
D | HOH522 |
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 | |