4FEU
Crystal structure of the aminoglycoside phosphotransferase APH(3')-Ia, with substrate kanamycin and small molecule inhibitor anthrapyrazolone SP600125
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005524 | molecular_function | ATP binding |
| A | 0016773 | molecular_function | phosphotransferase activity, alcohol group as acceptor |
| A | 0046677 | biological_process | response to antibiotic |
| B | 0005524 | molecular_function | ATP binding |
| B | 0016773 | molecular_function | phosphotransferase activity, alcohol group as acceptor |
| B | 0046677 | biological_process | response to antibiotic |
| C | 0005524 | molecular_function | ATP binding |
| C | 0016773 | molecular_function | phosphotransferase activity, alcohol group as acceptor |
| C | 0046677 | biological_process | response to antibiotic |
| D | 0005524 | molecular_function | ATP binding |
| D | 0016773 | molecular_function | phosphotransferase activity, alcohol group as acceptor |
| D | 0046677 | biological_process | response to antibiotic |
| E | 0005524 | molecular_function | ATP binding |
| E | 0016773 | molecular_function | phosphotransferase activity, alcohol group as acceptor |
| E | 0046677 | biological_process | response to antibiotic |
| F | 0005524 | molecular_function | ATP binding |
| F | 0016773 | molecular_function | phosphotransferase activity, alcohol group as acceptor |
| F | 0046677 | biological_process | response to antibiotic |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE KAN A 301 |
| Chain | Residue |
| A | ASP165 |
| A | GLU269 |
| A | PHE271 |
| A | HOH402 |
| A | HOH416 |
| A | HOH420 |
| A | HOH458 |
| A | HOH518 |
| B | SER2 |
| B | HIS3 |
| A | PHE166 |
| A | ASP167 |
| A | ASP198 |
| A | ARG219 |
| A | ASN234 |
| A | CYS235 |
| A | GLU238 |
| A | ASP268 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE 537 A 302 |
| Chain | Residue |
| A | PHE53 |
| A | PRO82 |
| A | THR98 |
| A | ILE101 |
| A | ILE215 |
| A | HOH486 |
| site_id | AC3 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE ACT A 303 |
| Chain | Residue |
| A | THR76 |
| A | MSE79 |
| site_id | AC4 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE KAN B 301 |
| Chain | Residue |
| B | ASP165 |
| B | PHE166 |
| B | ASP167 |
| B | ASP198 |
| B | ASN234 |
| B | GLU238 |
| B | ASP268 |
| B | GLU269 |
| B | PHE271 |
| B | HOH432 |
| B | HOH443 |
| B | HOH451 |
| B | HOH457 |
| B | HOH482 |
| B | HOH496 |
| B | HOH502 |
| B | HOH504 |
| B | HOH508 |
| C | GLY252 |
| C | ASP254 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE ACT B 302 |
| Chain | Residue |
| B | MSE79 |
| B | PRO80 |
| B | HOH535 |
| site_id | AC6 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE KAN C 301 |
| Chain | Residue |
| C | SER36 |
| C | ASP165 |
| C | ASP167 |
| C | ASP198 |
| C | ASN234 |
| C | CYS235 |
| C | ASP268 |
| C | GLU269 |
| C | PHE271 |
| C | HOH412 |
| C | HOH433 |
| C | HOH442 |
| C | HOH460 |
| C | HOH471 |
| C | HOH500 |
| C | HOH515 |
| C | HOH520 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE 537 C 302 |
| Chain | Residue |
| C | PHE53 |
| C | THR98 |
| C | ILE101 |
| C | THR105 |
| C | ILE205 |
| C | ILE215 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ACT C 303 |
| Chain | Residue |
| C | MSE156 |
| C | GLU176 |
| C | HOH529 |
| F | PRO241 |
| site_id | AC9 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE ACT C 304 |
| Chain | Residue |
| C | MSE79 |
| C | PRO80 |
| site_id | BC1 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE KAN D 301 |
| Chain | Residue |
| D | ASP165 |
| D | ASP167 |
| D | ASP198 |
| D | ASN234 |
| D | CYS235 |
| D | ASP268 |
| D | GLU269 |
| D | PHE271 |
| D | HOH403 |
| D | HOH404 |
| D | HOH411 |
| D | HOH413 |
| D | HOH414 |
| D | HOH430 |
| site_id | BC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE ACT D 302 |
| Chain | Residue |
| D | PHE78 |
| D | MSE79 |
| D | ARG130 |
| site_id | BC3 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE KAN E 301 |
| Chain | Residue |
| E | ASP167 |
| E | ASP198 |
| E | ARG219 |
| E | ASN234 |
| E | CYS235 |
| E | GLU238 |
| E | ASP268 |
| E | GLU269 |
| E | PHE271 |
| E | HOH437 |
| E | HOH475 |
| E | HOH492 |
| E | HOH495 |
| E | HOH501 |
| E | HOH504 |
| E | HOH516 |
| B | ARG6 |
| E | SER36 |
| E | ASP165 |
| E | PHE166 |
| site_id | BC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE 537 E 302 |
| Chain | Residue |
| E | PHE53 |
| E | THR98 |
| E | ILE101 |
| E | ILE205 |
| E | ILE215 |
| site_id | BC5 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE KAN F 301 |
| Chain | Residue |
| A | GLY252 |
| A | ASP254 |
| F | ASP165 |
| F | PHE166 |
| F | ASP167 |
| F | ASP198 |
| F | ASN234 |
| F | CYS235 |
| F | GLU238 |
| F | ASP268 |
| F | GLU269 |
| F | PHE271 |
| F | HOH401 |
| F | HOH407 |
| F | HOH408 |
| F | HOH413 |
| F | HOH426 |
| F | HOH438 |
| F | HOH459 |
| F | HOH461 |
| F | HOH466 |
| F | HOH473 |
| site_id | BC6 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE ACT F 302 |
| Chain | Residue |
| F | THR76 |
| F | MSE79 |
Functional Information from PROSITE/UniProt
| site_id | PS00109 |
| Number of Residues | 13 |
| Details | PROTEIN_KINASE_TYR Tyrosine protein kinases specific active-site signature. VTHgDFSLDNLIF |
| Chain | Residue | Details |
| A | VAL194-PHE206 |
