Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0008658 | molecular_function | penicillin binding |
A | 0008800 | molecular_function | beta-lactamase activity |
A | 0017001 | biological_process | antibiotic catabolic process |
B | 0008658 | molecular_function | penicillin binding |
B | 0008800 | molecular_function | beta-lactamase activity |
B | 0017001 | biological_process | antibiotic catabolic process |
C | 0008658 | molecular_function | penicillin binding |
C | 0008800 | molecular_function | beta-lactamase activity |
C | 0017001 | biological_process | antibiotic catabolic process |
D | 0008658 | molecular_function | penicillin binding |
D | 0008800 | molecular_function | beta-lactamase activity |
D | 0017001 | biological_process | antibiotic catabolic process |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 8 |
Details | binding site for residue EDO A 301 |
Chain | Residue |
A | GLN100 |
A | SER101 |
A | LEU189 |
A | GLY241 |
A | THR242 |
A | HOH402 |
A | HOH414 |
A | HOH416 |
site_id | AC2 |
Number of Residues | 5 |
Details | binding site for residue PEG A 302 |
Chain | Residue |
A | ALA116 |
A | ASP160 |
A | ARG165 |
A | HOH515 |
A | VAL114 |
site_id | AC3 |
Number of Residues | 9 |
Details | binding site for residue MLI B 301 |
Chain | Residue |
B | SER101 |
B | LYS104 |
B | GLU148 |
B | SER149 |
B | LYS239 |
B | THR240 |
B | GLY241 |
B | THR242 |
B | HOH476 |
site_id | AC4 |
Number of Residues | 4 |
Details | binding site for residue MLI B 302 |
Chain | Residue |
B | ALA208 |
B | LYS223 |
B | TYR237 |
B | SER259 |
site_id | AC5 |
Number of Residues | 5 |
Details | binding site for residue PEG B 303 |
Chain | Residue |
B | VAL114 |
B | ALA116 |
B | ASP160 |
B | ARG165 |
B | HOH569 |
site_id | AC6 |
Number of Residues | 9 |
Details | binding site for residue MLI D 301 |
Chain | Residue |
D | SER101 |
D | LYS104 |
D | GLU148 |
D | SER149 |
D | LYS239 |
D | THR240 |
D | GLY241 |
D | HOH421 |
D | HOH427 |
site_id | AC7 |
Number of Residues | 5 |
Details | binding site for residue EDO D 302 |
Chain | Residue |
C | ARG147 |
C | ILE227 |
C | GLN228 |
D | ARG224 |
D | HOH412 |
site_id | AC8 |
Number of Residues | 6 |
Details | binding site for residue EDO D 303 |
Chain | Residue |
D | MET146 |
D | ARG147 |
D | GLN228 |
D | LYS239 |
D | THR240 |
D | HOH456 |
site_id | AC9 |
Number of Residues | 3 |
Details | binding site for residue EDO D 304 |
Chain | Residue |
D | LYS223 |
D | LYS254 |
D | SER259 |
Functional Information from PROSITE/UniProt
site_id | PS00337 |
Number of Residues | 11 |
Details | BETA_LACTAMASE_D Beta-lactamase class-D active site. PqSTFKVVnAL |
Chain | Residue | Details |
B | PRO99-LEU109 | |
A | PRO99-LEU109 | |
Functional Information from SwissProt/UniProt
Chain | Residue | Details |
B | SER101 | |
D | SER101 | |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000250 |
Chain | Residue | Details |
B | LYS239 | |
D | LYS239 | |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | MOD_RES: N6-carboxylysine => ECO:0000250 |
Chain | Residue | Details |
B | LYS104 | |
D | LYS104 | |