5EPH
Crystal structure of extended-spectrum beta-lactamase BEL-1 in complex with Imipenem
Replaces: 4MXBFunctional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0008800 | molecular_function | beta-lactamase activity |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0017001 | biological_process | antibiotic catabolic process |
| A | 0030655 | biological_process | beta-lactam antibiotic catabolic process |
| A | 0046677 | biological_process | response to antibiotic |
| B | 0008800 | molecular_function | beta-lactamase activity |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0017001 | biological_process | antibiotic catabolic process |
| B | 0030655 | biological_process | beta-lactam antibiotic catabolic process |
| B | 0046677 | biological_process | response to antibiotic |
| C | 0008800 | molecular_function | beta-lactamase activity |
| C | 0016787 | molecular_function | hydrolase activity |
| C | 0017001 | biological_process | antibiotic catabolic process |
| C | 0030655 | biological_process | beta-lactam antibiotic catabolic process |
| C | 0046677 | biological_process | response to antibiotic |
| D | 0008800 | molecular_function | beta-lactamase activity |
| D | 0016787 | molecular_function | hydrolase activity |
| D | 0017001 | biological_process | antibiotic catabolic process |
| D | 0030655 | biological_process | beta-lactam antibiotic catabolic process |
| D | 0046677 | biological_process | response to antibiotic |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | binding site for residue CL A 301 |
| Chain | Residue |
| A | CYS61 |
| A | SER62 |
| A | THR63 |
| A | ASN237 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | binding site for residue CL A 302 |
| Chain | Residue |
| A | SER43 |
| A | ASN45 |
| B | LYS197 |
| site_id | AC3 |
| Number of Residues | 11 |
| Details | binding site for residue ID1 A 303 |
| Chain | Residue |
| A | LYS65 |
| A | TYR97 |
| A | SER123 |
| A | ASN125 |
| A | GLU159 |
| A | THR228 |
| A | GLY229 |
| A | SER230 |
| A | HOH495 |
| A | CYS61 |
| A | SER62 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | binding site for residue CL B 301 |
| Chain | Residue |
| B | CYS61 |
| B | SER62 |
| B | THR63 |
| B | ASN237 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | binding site for residue MRD B 303 |
| Chain | Residue |
| A | HIS283 |
| B | ALA59 |
| B | ASP169 |
| B | HOH462 |
| B | HOH466 |
| B | HOH467 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | binding site for residue CL C 301 |
| Chain | Residue |
| C | MET60 |
| C | CYS61 |
| C | SER62 |
| C | THR63 |
| C | ASN237 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | binding site for residue CL D 301 |
| Chain | Residue |
| D | CYS61 |
| D | SER62 |
| D | THR63 |
| D | ASN237 |
| site_id | AC8 |
| Number of Residues | 12 |
| Details | binding site for Di-peptide ID1 B 302 and SER B 62 |
| Chain | Residue |
| B | MET60 |
| B | CYS61 |
| B | THR63 |
| B | PHE64 |
| B | LYS65 |
| B | SER123 |
| B | ASN125 |
| B | THR228 |
| B | GLY229 |
| B | SER230 |
| B | CL301 |
| B | HOH421 |
| site_id | AC9 |
| Number of Residues | 16 |
| Details | binding site for Di-peptide ID1 C 302 and SER C 62 |
| Chain | Residue |
| C | MET60 |
| C | CYS61 |
| C | THR63 |
| C | PHE64 |
| C | LYS65 |
| C | TYR97 |
| C | SER123 |
| C | ASN125 |
| C | GLU159 |
| C | THR209 |
| C | LYS227 |
| C | THR228 |
| C | GLY229 |
| C | SER230 |
| C | CL301 |
| C | HOH429 |
| site_id | AD1 |
| Number of Residues | 14 |
| Details | binding site for Di-peptide ID1 D 302 and SER D 62 |
| Chain | Residue |
| D | MET60 |
| D | CYS61 |
| D | THR63 |
| D | PHE64 |
| D | LYS65 |
| D | TYR97 |
| D | SER123 |
| D | ASN125 |
| D | THR228 |
| D | GLY229 |
| D | SER230 |
| D | CL301 |
| D | HOH470 |
| D | HOH484 |
Functional Information from PROSITE/UniProt
| site_id | PS00146 |
| Number of Residues | 16 |
| Details | BETA_LACTAMASE_A Beta-lactamase class-A active site. FaMCSTfKlplAALVL |
| Chain | Residue | Details |
| A | PHE58-LEU73 |






