Functional 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 |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 5 |
Details | binding site for residue CL A 301 |
Chain | Residue |
A | GLU96 |
A | ALA98 |
A | PRO99 |
A | LYS102 |
B | HOH759 |
site_id | AC2 |
Number of Residues | 3 |
Details | binding site for residue EDO A 302 |
Chain | Residue |
A | HIS32 |
A | ASN33 |
A | GLN34 |
site_id | AC3 |
Number of Residues | 15 |
Details | binding site for residue CIT A 303 |
Chain | Residue |
A | LYS65 |
A | TYR97 |
A | SER123 |
A | ASN125 |
A | THR209 |
A | LYS227 |
A | THR228 |
A | GLY229 |
A | SER230 |
A | HOH454 |
A | HOH523 |
A | HOH530 |
A | HOH559 |
A | HOH566 |
A | SER62 |
site_id | AC4 |
Number of Residues | 12 |
Details | binding site for residue 1PE A 304 |
Chain | Residue |
A | ARG236 |
A | GLN262 |
A | GLY263 |
A | GLU264 |
A | GLU265 |
A | ALA267 |
A | LEU268 |
A | HOH458 |
A | HOH463 |
A | HOH494 |
A | HOH529 |
A | HOH674 |
site_id | AC5 |
Number of Residues | 6 |
Details | binding site for residue IPA A 305 |
Chain | Residue |
A | ARG201 |
A | ARG202 |
A | ILE205 |
A | HOH668 |
A | HOH709 |
B | THR107 |
site_id | AC6 |
Number of Residues | 4 |
Details | binding site for residue MRD A 306 |
Chain | Residue |
A | GLU23 |
A | TYR52 |
A | ARG53 |
A | HOH590 |
site_id | AC7 |
Number of Residues | 3 |
Details | binding site for residue CL A 307 |
Chain | Residue |
A | ARG236 |
A | ARG266 |
A | HOH506 |
site_id | AC8 |
Number of Residues | 3 |
Details | binding site for residue CL B 301 |
Chain | Residue |
A | LYS197 |
B | SER43 |
B | ASN45 |
site_id | AC9 |
Number of Residues | 5 |
Details | binding site for residue CL B 302 |
Chain | Residue |
A | HOH727 |
B | GLU96 |
B | ALA98 |
B | PRO99 |
B | LYS102 |
site_id | AD1 |
Number of Residues | 3 |
Details | binding site for residue CL B 303 |
Chain | Residue |
B | ARG236 |
B | ARG266 |
B | HOH489 |
site_id | AD2 |
Number of Residues | 13 |
Details | binding site for residue PGE B 304 |
Chain | Residue |
B | ASP90 |
B | ALA92 |
B | PHE93 |
B | LEU94 |
B | GLU95 |
B | HOH404 |
B | HOH405 |
B | HOH406 |
B | HOH415 |
B | HOH429 |
B | HOH614 |
B | HOH687 |
B | HOH691 |
site_id | AD3 |
Number of Residues | 5 |
Details | binding site for residue IPA B 305 |
Chain | Residue |
B | TYR52 |
B | ARG53 |
B | HOH469 |
B | HOH605 |
B | HOH740 |
site_id | AD4 |
Number of Residues | 9 |
Details | binding site for residue EDO B 306 |
Chain | Residue |
B | GLY149 |
B | ASP150 |
B | LYS151 |
B | VAL152 |
B | SER178 |
B | HOH447 |
B | HOH457 |
B | HOH656 |
B | HOH670 |
site_id | AD5 |
Number of Residues | 3 |
Details | binding site for residue EDO B 307 |
Chain | Residue |
B | THR166 |
B | PRO167 |
B | ASN233 |
site_id | AD6 |
Number of Residues | 15 |
Details | binding site for residue CIT B 308 |
Chain | Residue |
B | HOH514 |
B | HOH568 |
B | HOH575 |
B | HOH592 |
B | HOH651 |
B | SER62 |
B | TYR97 |
B | SER123 |
B | ASN125 |
B | THR209 |
B | LYS227 |
B | THR228 |
B | GLY229 |
B | SER230 |
B | HOH463 |
site_id | AD7 |
Number of Residues | 3 |
Details | binding site for residue CL B 309 |
Chain | Residue |
B | ASP90 |
B | SER91 |
B | HOH720 |
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 | |