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 |