6MN4
Crystal structure of aminoglycoside acetyltransferase AAC(3)-IVa, H154A mutant, in complex with apramycin
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0008080 | molecular_function | N-acetyltransferase activity |
| A | 0016746 | molecular_function | acyltransferase activity |
| A | 0046353 | molecular_function | aminoglycoside 3-N-acetyltransferase activity |
| A | 0046677 | biological_process | response to antibiotic |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0008080 | molecular_function | N-acetyltransferase activity |
| B | 0016746 | molecular_function | acyltransferase activity |
| B | 0046353 | molecular_function | aminoglycoside 3-N-acetyltransferase activity |
| B | 0046677 | biological_process | response to antibiotic |
| B | 0046872 | molecular_function | metal ion binding |
| C | 0008080 | molecular_function | N-acetyltransferase activity |
| C | 0016746 | molecular_function | acyltransferase activity |
| C | 0046353 | molecular_function | aminoglycoside 3-N-acetyltransferase activity |
| C | 0046677 | biological_process | response to antibiotic |
| C | 0046872 | molecular_function | metal ion binding |
| D | 0008080 | molecular_function | N-acetyltransferase activity |
| D | 0016746 | molecular_function | acyltransferase activity |
| D | 0046353 | molecular_function | aminoglycoside 3-N-acetyltransferase activity |
| D | 0046677 | biological_process | response to antibiotic |
| D | 0046872 | molecular_function | metal ion binding |
| E | 0008080 | molecular_function | N-acetyltransferase activity |
| E | 0016746 | molecular_function | acyltransferase activity |
| E | 0046353 | molecular_function | aminoglycoside 3-N-acetyltransferase activity |
| E | 0046677 | biological_process | response to antibiotic |
| E | 0046872 | molecular_function | metal ion binding |
| F | 0008080 | molecular_function | N-acetyltransferase activity |
| F | 0016746 | molecular_function | acyltransferase activity |
| F | 0046353 | molecular_function | aminoglycoside 3-N-acetyltransferase activity |
| F | 0046677 | biological_process | response to antibiotic |
| F | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 13 |
| Details | binding site for residue AM2 A 301 |
| Chain | Residue |
| A | TRP63 |
| A | HOH406 |
| A | HOH421 |
| A | HOH430 |
| A | HOH432 |
| A | ASP67 |
| A | HIS124 |
| A | ARG168 |
| A | HIS169 |
| A | GLU185 |
| A | ASP187 |
| A | HIS188 |
| A | GLU249 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | binding site for residue ZN A 302 |
| Chain | Residue |
| A | CYS189 |
| A | HIS241 |
| A | CYS247 |
| A | CYS250 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | binding site for residue EDO A 303 |
| Chain | Residue |
| A | LYS7 |
| A | GLU46 |
| A | ALA50 |
| site_id | AC4 |
| Number of Residues | 2 |
| Details | binding site for residue EDO A 304 |
| Chain | Residue |
| A | ASP39 |
| A | GLU46 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | binding site for residue EDO A 305 |
| Chain | Residue |
| A | PRO73 |
| A | LYS96 |
| A | ARG97 |
| site_id | AC6 |
| Number of Residues | 1 |
| Details | binding site for residue EDO A 306 |
| Chain | Residue |
| A | LEU121 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | binding site for residue PO4 A 307 |
| Chain | Residue |
| A | SER30 |
| A | PHE31 |
| A | ARG32 |
| A | GLY83 |
| A | VAL84 |
| site_id | AC8 |
| Number of Residues | 7 |
| Details | binding site for residue EPE A 308 |
| Chain | Residue |
| A | PHE31 |
| A | ARG35 |
| A | PRO36 |
| A | LEU37 |
| A | GLU38 |
| A | GLY40 |
| B | ALA74 |
| site_id | AC9 |
| Number of Residues | 10 |
| Details | binding site for residue AM2 B 301 |
| Chain | Residue |
| B | TRP63 |
| B | ASP67 |
| B | HIS124 |
| B | PRO167 |
| B | ARG168 |
| B | HIS169 |
| B | GLU185 |
| B | ASP187 |
| B | GLU249 |
| B | HOH412 |
| site_id | AD1 |
| Number of Residues | 4 |
| Details | binding site for residue ZN B 302 |
| Chain | Residue |
| B | CYS189 |
| B | HIS241 |
| B | CYS247 |
| B | CYS250 |
| site_id | AD2 |
| Number of Residues | 4 |
| Details | binding site for residue EDO B 303 |
| Chain | Residue |
| B | ARG192 |
| B | ASP235 |
| B | LEU237 |
| B | LEU240 |
| site_id | AD3 |
| Number of Residues | 6 |
| Details | binding site for residue PO4 B 304 |
| Chain | Residue |
| B | SER30 |
| B | PHE31 |
| B | ARG32 |
| B | GLY83 |
| B | VAL84 |
| B | HOH403 |
| site_id | AD4 |
| Number of Residues | 8 |
| Details | binding site for residue EPE B 305 |
| Chain | Residue |
| A | ALA74 |
| B | GLU4 |
| B | PHE31 |
| B | ARG35 |
| B | PRO36 |
| B | LEU37 |
| B | GLU38 |
| B | GLY40 |
| site_id | AD5 |
| Number of Residues | 9 |
| Details | binding site for residue AM2 C 301 |
| Chain | Residue |
| C | TRP63 |
| C | ASP67 |
| C | HIS124 |
| C | ARG168 |
| C | HIS169 |
| C | GLU185 |
| C | ASP187 |
| C | HIS188 |
| C | HOH412 |
| site_id | AD6 |
| Number of Residues | 4 |
| Details | binding site for residue ZN C 302 |
| Chain | Residue |
| C | CYS189 |
| C | HIS241 |
| C | CYS247 |
| C | CYS250 |
| site_id | AD7 |
| Number of Residues | 5 |
| Details | binding site for residue PO4 C 303 |
| Chain | Residue |
| C | SER30 |
| C | PHE31 |
| C | ARG32 |
| C | GLY83 |
| C | VAL84 |
| site_id | AD8 |
| Number of Residues | 7 |
| Details | binding site for residue EPE C 304 |
| Chain | Residue |
| C | GLU4 |
| C | PHE31 |
| C | ARG35 |
| C | PRO36 |
| C | LEU37 |
| C | GLU38 |
| C | GLY40 |
| site_id | AD9 |
| Number of Residues | 10 |
| Details | binding site for residue AM2 D 301 |
| Chain | Residue |
| D | HIS169 |
| D | GLU185 |
| D | ASP187 |
| D | GLU249 |
| D | HOH404 |
| D | HOH411 |
| D | TRP63 |
| D | ASP67 |
| D | HIS124 |
| D | ARG168 |
| site_id | AE1 |
| Number of Residues | 4 |
| Details | binding site for residue ZN D 302 |
| Chain | Residue |
| D | CYS189 |
| D | HIS241 |
| D | CYS247 |
| D | CYS250 |
| site_id | AE2 |
| Number of Residues | 6 |
| Details | binding site for residue PO4 D 303 |
| Chain | Residue |
| D | SER30 |
| D | PHE31 |
| D | ARG32 |
| D | GLY83 |
| D | VAL84 |
| D | HOH403 |
| site_id | AE3 |
| Number of Residues | 3 |
| Details | binding site for residue GOL D 304 |
| Chain | Residue |
| C | PRO236 |
| D | ARG198 |
| D | ARG234 |
| site_id | AE4 |
| Number of Residues | 7 |
| Details | binding site for residue EPE D 305 |
| Chain | Residue |
| D | GLU4 |
| D | PHE31 |
| D | ARG35 |
| D | PRO36 |
| D | LEU37 |
| D | GLU38 |
| D | GLY40 |
| site_id | AE5 |
| Number of Residues | 8 |
| Details | binding site for residue AM2 E 301 |
| Chain | Residue |
| E | TRP63 |
| E | HIS124 |
| E | THR151 |
| E | ARG168 |
| E | HIS169 |
| E | GLU185 |
| E | ASP187 |
| E | HIS188 |
| site_id | AE6 |
| Number of Residues | 2 |
| Details | binding site for residue EDO E 302 |
| Chain | Residue |
| E | LYS96 |
| E | ARG97 |
| site_id | AE7 |
| Number of Residues | 5 |
| Details | binding site for residue PO4 E 303 |
| Chain | Residue |
| E | SER30 |
| E | PHE31 |
| E | ARG32 |
| E | GLY83 |
| E | VAL84 |
| site_id | AE8 |
| Number of Residues | 1 |
| Details | binding site for residue GOL E 304 |
| Chain | Residue |
| E | THR75 |
| site_id | AE9 |
| Number of Residues | 8 |
| Details | binding site for residue EPE E 305 |
| Chain | Residue |
| D | ALA74 |
| E | GLU4 |
| E | PHE31 |
| E | ARG35 |
| E | PRO36 |
| E | LEU37 |
| E | GLU38 |
| E | GLY40 |
| site_id | AF1 |
| Number of Residues | 8 |
| Details | binding site for residue AM2 F 301 |
| Chain | Residue |
| F | TRP63 |
| F | HIS124 |
| F | ARG168 |
| F | HIS169 |
| F | GLU185 |
| F | ASP187 |
| F | HIS188 |
| F | GLU249 |
| site_id | AF2 |
| Number of Residues | 7 |
| Details | binding site for residue PO4 F 302 |
| Chain | Residue |
| F | PHE31 |
| F | ARG32 |
| F | GLY83 |
| F | VAL84 |
| F | HOH401 |
| F | HOH408 |
| F | HOH413 |
| site_id | AF3 |
| Number of Residues | 4 |
| Details | binding site for residue EPE F 303 |
| Chain | Residue |
| F | PHE31 |
| F | ARG35 |
| F | PRO36 |
| F | LEU37 |
