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 |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 11 |
Details | binding site for residue KE1 A 301 |
Chain | Residue |
A | ALA69 |
A | HOH517 |
A | HOH530 |
A | SER70 |
A | SER118 |
A | VAL120 |
A | LEU158 |
A | THR209 |
A | GLY210 |
A | TYR211 |
A | ARG250 |
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 | 2 |
Details | binding site for residue CL A 303 |
Chain | Residue |
A | ARG206 |
B | ARG206 |
site_id | AC4 |
Number of Residues | 5 |
Details | binding site for residue CA A 304 |
Chain | Residue |
A | GLU37 |
A | HIS38 |
A | GLU256 |
A | HOH506 |
A | HOH544 |
site_id | AC5 |
Number of Residues | 2 |
Details | binding site for residue CA A 305 |
Chain | Residue |
A | GLU27 |
A | HOH529 |
site_id | AC6 |
Number of Residues | 6 |
Details | binding site for residue CD A 306 |
Chain | Residue |
A | GLU37 |
A | GLU125 |
A | GLU256 |
A | HOH401 |
A | HOH506 |
A | HOH550 |
site_id | AC7 |
Number of Residues | 2 |
Details | binding site for residue CL B 302 |
Chain | Residue |
B | LYS73 |
B | TRP157 |
site_id | AC8 |
Number of Residues | 5 |
Details | binding site for residue CL B 303 |
Chain | Residue |
A | HOH558 |
B | HOH413 |
B | HOH505 |
B | HOH507 |
B | HOH514 |
site_id | AC9 |
Number of Residues | 4 |
Details | binding site for residue CL B 304 |
Chain | Residue |
A | HOH557 |
A | HOH561 |
B | HOH499 |
B | HOH508 |
site_id | AD1 |
Number of Residues | 6 |
Details | binding site for residue CA B 305 |
Chain | Residue |
A | ASP143 |
A | GLU147 |
A | HOH412 |
B | ASP143 |
B | GLU147 |
B | HOH421 |
site_id | AD2 |
Number of Residues | 6 |
Details | binding site for residue CD B 306 |
Chain | Residue |
A | GLU147 |
B | ASP143 |
B | HOH402 |
B | HOH465 |
B | HOH468 |
B | HOH502 |
site_id | AD3 |
Number of Residues | 14 |
Details | binding site for Di-peptide KE1 B 301 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 | HOH495 |
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 | |