6CYQ
Crystal structure of CTX-M-14 S70G/N106S beta-lactamase in complex with hydrolyzed cefotaxime
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 |
| 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 |
| E | 0008800 | molecular_function | beta-lactamase activity |
| E | 0016787 | molecular_function | hydrolase activity |
| E | 0017001 | biological_process | antibiotic catabolic process |
| E | 0030655 | biological_process | beta-lactam antibiotic catabolic process |
| E | 0046677 | biological_process | response to antibiotic |
| F | 0008800 | molecular_function | beta-lactamase activity |
| F | 0016787 | molecular_function | hydrolase activity |
| F | 0017001 | biological_process | antibiotic catabolic process |
| F | 0030655 | biological_process | beta-lactam antibiotic catabolic process |
| F | 0046677 | biological_process | response to antibiotic |
| G | 0008800 | molecular_function | beta-lactamase activity |
| G | 0016787 | molecular_function | hydrolase activity |
| G | 0017001 | biological_process | antibiotic catabolic process |
| G | 0030655 | biological_process | beta-lactam antibiotic catabolic process |
| G | 0046677 | biological_process | response to antibiotic |
| H | 0008800 | molecular_function | beta-lactamase activity |
| H | 0016787 | molecular_function | hydrolase activity |
| H | 0017001 | biological_process | antibiotic catabolic process |
| H | 0030655 | biological_process | beta-lactam antibiotic catabolic process |
| H | 0046677 | biological_process | response to antibiotic |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 17 |
| Details | binding site for residue CE4 A 301 |
| Chain | Residue |
| A | CYS69 |
| A | THR235 |
| A | GLY236 |
| A | SER237 |
| A | GLY238 |
| A | ASP240 |
| A | HOH406 |
| A | HOH432 |
| A | HOH440 |
| A | GLY70 |
| A | LYS73 |
| A | TYR105 |
| A | SER130 |
| A | ASN132 |
| A | PRO167 |
| A | ASN170 |
| A | LYS234 |
| site_id | AC2 |
| Number of Residues | 18 |
| Details | binding site for residue CE4 B 301 |
| Chain | Residue |
| B | CYS69 |
| B | GLY70 |
| B | LYS73 |
| B | TYR105 |
| B | SER130 |
| B | ASN132 |
| B | PRO167 |
| B | ASN170 |
| B | LYS234 |
| B | THR235 |
| B | GLY236 |
| B | SER237 |
| B | GLY238 |
| B | ASP240 |
| B | HOH402 |
| B | HOH403 |
| B | HOH424 |
| B | HOH481 |
| site_id | AC3 |
| Number of Residues | 20 |
| Details | binding site for residue CE4 C 301 |
| Chain | Residue |
| C | CYS69 |
| C | GLY70 |
| C | LYS73 |
| C | TYR105 |
| C | SER130 |
| C | ASN132 |
| C | GLU166 |
| C | PRO167 |
| C | ASN170 |
| C | LYS234 |
| C | THR235 |
| C | GLY236 |
| C | SER237 |
| C | GLY238 |
| C | ASP240 |
| C | HOH401 |
| C | HOH407 |
| C | HOH410 |
| C | HOH418 |
| C | HOH436 |
| site_id | AC4 |
| Number of Residues | 18 |
| Details | binding site for residue CE4 D 301 |
| Chain | Residue |
| D | CYS69 |
| D | GLY70 |
| D | LYS73 |
| D | TYR105 |
| D | SER130 |
| D | ASN132 |
| D | PRO167 |
| D | ASN170 |
| D | LYS234 |
| D | THR235 |
| D | GLY236 |
| D | SER237 |
| D | GLY238 |
| D | ASP240 |
| D | HOH408 |
| D | HOH430 |
| D | HOH435 |
| D | HOH492 |
| site_id | AC5 |
| Number of Residues | 19 |
| Details | binding site for residue CE4 E 301 |
| Chain | Residue |
| E | CYS69 |
| E | GLY70 |
| E | LYS73 |
| E | TYR105 |
| E | SER130 |
| E | ASN132 |
| E | PRO167 |
| E | ASN170 |
| E | LYS234 |
| E | THR235 |
| E | GLY236 |
| E | SER237 |
| E | GLY238 |
| E | ASP240 |
| E | HOH403 |
| E | HOH416 |
| E | HOH422 |
| E | HOH485 |
| E | HOH519 |
| site_id | AC6 |
| Number of Residues | 21 |
| Details | binding site for residue CE4 F 301 |
| Chain | Residue |
| F | ASN170 |
| F | LYS234 |
| F | THR235 |
| F | GLY236 |
| F | SER237 |
| F | GLY238 |
| F | ASP240 |
| F | HOH403 |
| F | HOH406 |
| F | HOH409 |
| F | HOH430 |
| F | HOH491 |
| F | HOH525 |
| F | HOH638 |
| F | CYS69 |
| F | GLY70 |
| F | LYS73 |
| F | TYR105 |
| F | SER130 |
| F | ASN132 |
| F | PRO167 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | binding site for residue GOL F 302 |
| Chain | Residue |
| F | THR202 |
| F | ALA205 |
| F | GLN206 |
| F | THR209 |
| F | HOH456 |
| H | GLN270 |
| site_id | AC8 |
| Number of Residues | 17 |
| Details | binding site for residue CE4 G 301 |
| Chain | Residue |
| G | CYS69 |
| G | GLY70 |
| G | LYS73 |
| G | TYR105 |
| G | SER130 |
| G | ASN132 |
| G | PRO167 |
| G | ASN170 |
| G | LYS234 |
| G | THR235 |
| G | GLY236 |
| G | SER237 |
| G | ASP240 |
| G | HOH406 |
| G | HOH417 |
| G | HOH456 |
| G | HOH498 |
| site_id | AC9 |
| Number of Residues | 17 |
| Details | binding site for residue CE4 H 301 |
| Chain | Residue |
| H | CYS69 |
| H | GLY70 |
| H | LYS73 |
| H | TYR105 |
| H | SER130 |
| H | ASN132 |
| H | PRO167 |
| H | ASN170 |
| H | LYS234 |
| H | THR235 |
| H | GLY236 |
| H | SER237 |
| H | ASP240 |
| H | HOH407 |
| H | HOH437 |
| H | HOH507 |
| H | HOH524 |
