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 |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 14 |
Details | binding site for residue QP2 A 301 |
Chain | Residue |
A | SER67 |
A | PRO245 |
A | ARG247 |
A | HOH401 |
A | HOH402 |
A | HOH469 |
A | KCX70 |
A | TRP102 |
A | SER115 |
A | VAL117 |
A | LYS205 |
A | THR206 |
A | GLY207 |
A | LEU244 |
site_id | AC2 |
Number of Residues | 7 |
Details | binding site for residue EDO A 302 |
Chain | Residue |
A | ARG125 |
A | LYS138 |
A | ASP151 |
A | HOH403 |
A | HOH430 |
A | HOH514 |
A | HOH620 |
site_id | AC3 |
Number of Residues | 2 |
Details | binding site for residue EDO A 303 |
Chain | Residue |
A | ARG160 |
A | HOH675 |
site_id | AC4 |
Number of Residues | 6 |
Details | binding site for residue EDO A 304 |
Chain | Residue |
A | THR107 |
A | ARG109 |
B | GLU224 |
B | GLU226 |
B | HOH421 |
B | HOH438 |
site_id | AC5 |
Number of Residues | 5 |
Details | binding site for residue EDO A 305 |
Chain | Residue |
A | LYS95 |
A | SER140 |
A | GLN144 |
A | HOH487 |
A | HOH512 |
site_id | AC6 |
Number of Residues | 3 |
Details | binding site for residue EDO A 306 |
Chain | Residue |
A | TYR200 |
A | ILE260 |
A | HOH438 |
site_id | AC7 |
Number of Residues | 5 |
Details | binding site for residue EDO A 307 |
Chain | Residue |
A | ARG125 |
A | SO4308 |
A | HOH403 |
A | HOH414 |
A | HOH590 |
site_id | AC8 |
Number of Residues | 11 |
Details | binding site for residue SO4 A 308 |
Chain | Residue |
A | ARG97 |
A | PRO118 |
A | LYS137 |
A | EDO307 |
A | HOH437 |
A | HOH474 |
A | HOH477 |
A | HOH493 |
A | HOH498 |
A | HOH565 |
A | HOH590 |
site_id | AC9 |
Number of Residues | 3 |
Details | binding site for residue CL A 309 |
Chain | Residue |
A | GLN121 |
A | LYS134 |
A | ARG211 |
site_id | AD1 |
Number of Residues | 6 |
Details | binding site for residue SO4 B 301 |
Chain | Residue |
B | ARG58 |
B | LYS61 |
B | HOH408 |
B | HOH440 |
B | HOH444 |
B | HOH493 |
Functional Information from PROSITE/UniProt
site_id | PS00337 |
Number of Residues | 11 |
Details | BETA_LACTAMASE_D Beta-lactamase class-D active site. PaSTFKIPnAI |
Chain | Residue | Details |
A | PRO65-ILE75 | |