6S0U
The crystal structure of kanamycin B dioxygenase (KanJ) from Streptomyces kanamyceticus in complex with nickel and 2-oxoglutarate
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0016706 | molecular_function | 2-oxoglutarate-dependent dioxygenase activity |
| A | 0017000 | biological_process | antibiotic biosynthetic process |
| A | 1901133 | biological_process | kanamycin biosynthetic process |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0016706 | molecular_function | 2-oxoglutarate-dependent dioxygenase activity |
| B | 0017000 | biological_process | antibiotic biosynthetic process |
| B | 1901133 | biological_process | kanamycin biosynthetic process |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0016706 | molecular_function | 2-oxoglutarate-dependent dioxygenase activity |
| C | 0017000 | biological_process | antibiotic biosynthetic process |
| C | 1901133 | biological_process | kanamycin biosynthetic process |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0016706 | molecular_function | 2-oxoglutarate-dependent dioxygenase activity |
| D | 0017000 | biological_process | antibiotic biosynthetic process |
| D | 1901133 | biological_process | kanamycin biosynthetic process |
| E | 0016491 | molecular_function | oxidoreductase activity |
| E | 0016706 | molecular_function | 2-oxoglutarate-dependent dioxygenase activity |
| E | 0017000 | biological_process | antibiotic biosynthetic process |
| E | 1901133 | biological_process | kanamycin biosynthetic process |
| F | 0016491 | molecular_function | oxidoreductase activity |
| F | 0016706 | molecular_function | 2-oxoglutarate-dependent dioxygenase activity |
| F | 0017000 | biological_process | antibiotic biosynthetic process |
| F | 1901133 | biological_process | kanamycin biosynthetic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 13 |
| Details | binding site for residue AKG A 301 |
| Chain | Residue |
| A | ASN73 |
| A | NI302 |
| A | HOH404 |
| A | HOH454 |
| A | HOH460 |
| A | ASN120 |
| A | GLN129 |
| A | HIS132 |
| A | ASP134 |
| A | THR165 |
| A | HIS219 |
| A | GLY221 |
| A | ARG230 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | binding site for residue NI A 302 |
| Chain | Residue |
| A | HIS132 |
| A | ASP134 |
| A | HIS219 |
| A | AKG301 |
| A | HOH404 |
| site_id | AC3 |
| Number of Residues | 13 |
| Details | binding site for residue AKG B 301 |
| Chain | Residue |
| B | ASN73 |
| B | ASN120 |
| B | GLN129 |
| B | HIS132 |
| B | ASP134 |
| B | THR165 |
| B | HIS219 |
| B | GLY221 |
| B | ARG230 |
| B | NI302 |
| B | HOH413 |
| B | HOH439 |
| B | HOH511 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | binding site for residue NI B 302 |
| Chain | Residue |
| B | HIS132 |
| B | ASP134 |
| B | HIS219 |
| B | AKG301 |
| B | HOH413 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | binding site for residue PEG B 303 |
| Chain | Residue |
| B | GLY259 |
| B | SER260 |
| B | ASP261 |
| B | HIS263 |
| B | HOH525 |
| site_id | AC6 |
| Number of Residues | 15 |
| Details | binding site for residue AKG C 301 |
| Chain | Residue |
| C | ASN73 |
| C | ASN120 |
| C | GLN129 |
| C | HIS132 |
| C | ASP134 |
| C | THR165 |
| C | HIS219 |
| C | GLY221 |
| C | ARG230 |
| C | NI302 |
| C | HOH406 |
| C | HOH422 |
| C | HOH441 |
| C | HOH453 |
| C | HOH523 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | binding site for residue NI C 302 |
| Chain | Residue |
| C | HIS132 |
| C | ASP134 |
| C | HIS219 |
| C | AKG301 |
| C | HOH422 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | binding site for residue CL C 303 |
| Chain | Residue |
| C | LEU187 |
| C | PRO188 |
| C | ALA189 |
| F | HOH492 |
| site_id | AC9 |
| Number of Residues | 13 |
| Details | binding site for residue AKG D 301 |
| Chain | Residue |
| D | ASN73 |
| D | ASN120 |
| D | GLN129 |
| D | HIS132 |
| D | ASP134 |
| D | THR165 |
| D | HIS219 |
| D | ARG230 |
| D | NI302 |
| D | HOH402 |
| D | HOH425 |
| D | HOH427 |
| D | HOH514 |
| site_id | AD1 |
| Number of Residues | 5 |
| Details | binding site for residue NI D 302 |
| Chain | Residue |
| D | HIS132 |
| D | ASP134 |
| D | HIS219 |
| D | AKG301 |
| D | HOH402 |
| site_id | AD2 |
| Number of Residues | 14 |
| Details | binding site for residue AKG E 301 |
| Chain | Residue |
| E | ASN73 |
| E | ASN120 |
| E | GLN129 |
| E | HIS132 |
| E | ASP134 |
| E | THR165 |
| E | HIS219 |
| E | GLY221 |
| E | ARG230 |
| E | NI302 |
| E | HOH412 |
| E | HOH414 |
| E | HOH469 |
| E | HOH478 |
| site_id | AD3 |
| Number of Residues | 5 |
| Details | binding site for residue NI E 302 |
| Chain | Residue |
| E | HIS219 |
| E | AKG301 |
| E | HOH412 |
| E | HIS132 |
| E | ASP134 |
| site_id | AD4 |
| Number of Residues | 4 |
| Details | binding site for residue CL E 303 |
| Chain | Residue |
| B | PRO188 |
| B | ALA189 |
| E | GLY77 |
| E | HOH549 |
| site_id | AD5 |
| Number of Residues | 6 |
| Details | binding site for residue NA E 304 |
| Chain | Residue |
| E | PRO16 |
| E | ASP18 |
| E | HOH420 |
| E | HOH441 |
| E | HOH447 |
| E | HOH471 |
| site_id | AD6 |
| Number of Residues | 12 |
| Details | binding site for residue AKG F 301 |
| Chain | Residue |
| F | ASN73 |
| F | ASN120 |
| F | GLN129 |
| F | HIS132 |
| F | ASP134 |
| F | THR165 |
| F | HIS219 |
| F | ARG230 |
| F | NI302 |
| F | HOH408 |
| F | HOH419 |
| F | HOH463 |
| site_id | AD7 |
| Number of Residues | 5 |
| Details | binding site for residue NI F 302 |
| Chain | Residue |
| F | HIS132 |
| F | ASP134 |
| F | HIS219 |
| F | AKG301 |
| F | HOH408 |
| site_id | AD8 |
| Number of Residues | 2 |
| Details | binding site for residue PEG F 303 |
| Chain | Residue |
| F | THR20 |
| F | ASP22 |
