6C5U
Aminoglycoside Phosphotransferase (2'')-Ia in complex with GMPPNP, Magnesium, and Ribostamycin, Alternate form
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 25 |
| Details | binding site for residue GNP A 500 |
| Chain | Residue |
| A | GLY211 |
| A | HIS379 |
| A | ILE392 |
| A | ASP393 |
| A | MG700 |
| A | MG702 |
| A | HOH900 |
| A | HOH901 |
| A | HOH903 |
| A | HOH904 |
| A | HOH906 |
| A | SER214 |
| A | HOH921 |
| A | HOH923 |
| A | HOH1091 |
| A | HOH1124 |
| A | HOH1154 |
| A | HOH1221 |
| A | ILE224 |
| A | LYS226 |
| A | TYR237 |
| A | TYR274 |
| A | GLU276 |
| A | ILE277 |
| A | PHE281 |
| site_id | AC2 |
| Number of Residues | 9 |
| Details | binding site for residue RIO A 600 |
| Chain | Residue |
| A | ASP374 |
| A | SER376 |
| A | TYR408 |
| A | GLU411 |
| A | GLU415 |
| A | GLU416 |
| A | GLU445 |
| A | HOH972 |
| A | HOH1426 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | binding site for residue MG A 700 |
| Chain | Residue |
| A | HIS379 |
| A | ASP393 |
| A | GNP500 |
| A | HOH900 |
| A | HOH901 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | binding site for residue MG A 702 |
| Chain | Residue |
| A | ASP393 |
| A | GNP500 |
| A | HOH902 |
| A | HOH903 |
| A | HOH904 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | binding site for residue CL A 802 |
| Chain | Residue |
| A | GLN462 |
| A | GLU466 |
| A | ARG469 |
| site_id | AC6 |
| Number of Residues | 19 |
| Details | binding site for residue GNP B 500 |
| Chain | Residue |
| B | SER214 |
| B | ILE224 |
| B | LYS226 |
| B | TYR237 |
| B | TYR274 |
| B | GLU276 |
| B | ILE277 |
| B | PHE281 |
| B | HIS379 |
| B | ASP393 |
| B | MG700 |
| B | MG702 |
| B | HOH900 |
| B | HOH901 |
| B | HOH903 |
| B | HOH904 |
| B | HOH906 |
| B | HOH921 |
| B | HOH923 |
| site_id | AC7 |
| Number of Residues | 10 |
| Details | binding site for residue RIO B 600 |
| Chain | Residue |
| B | ASP374 |
| B | SER376 |
| B | TYR408 |
| B | GLU411 |
| B | GLU415 |
| B | GLU416 |
| B | GLU445 |
| B | TYR448 |
| B | HOH1260 |
| B | HOH1325 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | binding site for residue MG B 700 |
| Chain | Residue |
| B | HIS379 |
| B | ASP393 |
| B | GNP500 |
| B | HOH900 |
| B | HOH901 |
| site_id | AC9 |
| Number of Residues | 5 |
| Details | binding site for residue MG B 702 |
| Chain | Residue |
| B | ASP393 |
| B | GNP500 |
| B | HOH902 |
| B | HOH903 |
| B | HOH904 |
| site_id | AD1 |
| Number of Residues | 3 |
| Details | binding site for residue CL B 802 |
| Chain | Residue |
| B | GLN462 |
| B | GLU466 |
| B | ARG469 |
| site_id | AD2 |
| Number of Residues | 22 |
| Details | binding site for residue GNP C 500 |
| Chain | Residue |
| C | ASP393 |
| C | MG700 |
| C | MG702 |
| C | HOH900 |
| C | HOH901 |
| C | HOH903 |
| C | HOH904 |
| C | HOH906 |
| C | HOH911 |
| C | HOH923 |
| C | HOH1038 |
| C | HOH1093 |
| C | GLY211 |
| C | SER214 |
| C | ILE224 |
| C | LYS226 |
| C | TYR237 |
| C | TYR274 |
| C | GLU276 |
| C | ILE277 |
| C | PHE281 |
| C | HIS379 |
| site_id | AD3 |
| Number of Residues | 5 |
| Details | binding site for residue MG C 700 |
| Chain | Residue |
| C | HIS379 |
| C | ASP393 |
| C | GNP500 |
| C | HOH900 |
| C | HOH901 |
| site_id | AD4 |
| Number of Residues | 5 |
| Details | binding site for residue MG C 702 |
| Chain | Residue |
| C | ASP393 |
| C | GNP500 |
| C | HOH902 |
| C | HOH903 |
| C | HOH904 |
| site_id | AD5 |
| Number of Residues | 3 |
| Details | binding site for residue CL C 802 |
| Chain | Residue |
| C | GLN462 |
| C | GLU466 |
| C | ARG469 |
| site_id | AD6 |
| Number of Residues | 19 |
| Details | binding site for residue GNP D 500 |
| Chain | Residue |
| D | SER214 |
| D | ILE224 |
| D | LYS226 |
| D | TYR274 |
| D | GLU276 |
| D | ILE277 |
| D | PHE281 |
| D | ASP374 |
| D | HIS379 |
| D | ILE392 |
| D | ASP393 |
| D | MG700 |
| D | MG702 |
| D | HOH900 |
| D | HOH902 |
| D | HOH906 |
| D | HOH911 |
| D | HOH923 |
| D | HOH1299 |
| site_id | AD7 |
| Number of Residues | 10 |
| Details | binding site for residue RIO D 600 |
| Chain | Residue |
| D | ASP374 |
| D | SER376 |
| D | TYR408 |
| D | GLU411 |
| D | SER413 |
| D | GLU415 |
| D | GLU416 |
| D | GLU445 |
| D | TYR448 |
| D | HOH1029 |
| site_id | AD8 |
| Number of Residues | 4 |
| Details | binding site for residue MG D 700 |
| Chain | Residue |
| D | HIS379 |
| D | ASP393 |
| D | GNP500 |
| D | HOH900 |
| site_id | AD9 |
| Number of Residues | 5 |
| Details | binding site for residue MG D 702 |
| Chain | Residue |
| D | LYS226 |
| D | ASP393 |
| D | GNP500 |
| D | HOH902 |
| D | HOH903 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | ACT_SITE: Proton acceptor; for phosphotransferase activity => ECO:0000250 |
| Chain | Residue | Details |
| A | ASP374 | |
| B | ASP374 | |
| C | ASP374 | |
| D | ASP374 | |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000250 |
| Chain | Residue | Details |
| A | ASP393 | |
| B | ASP393 | |
| C | ASP393 | |
| D | ASP393 | |
