Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0005524 | molecular_function | ATP binding |
| A | 0008910 | molecular_function | kanamycin kinase activity |
| A | 0016301 | molecular_function | kinase activity |
| A | 0016740 | molecular_function | transferase activity |
| A | 0016773 | molecular_function | phosphotransferase activity, alcohol group as acceptor |
| A | 0046677 | biological_process | response to antibiotic |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0005524 | molecular_function | ATP binding |
| B | 0008910 | molecular_function | kanamycin kinase activity |
| B | 0016301 | molecular_function | kinase activity |
| B | 0016740 | molecular_function | transferase activity |
| B | 0016773 | molecular_function | phosphotransferase activity, alcohol group as acceptor |
| B | 0046677 | biological_process | response to antibiotic |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG A 301 |
| Chain | Residue |
| A | ASN195 |
| A | ASP208 |
| A | MG302 |
| A | ADP303 |
| A | HOH438 |
| A | HOH482 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG A 302 |
| Chain | Residue |
| A | HOH423 |
| A | HOH479 |
| A | HOH483 |
| A | ASP208 |
| A | MG301 |
| A | ADP303 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG B 301 |
| Chain | Residue |
| B | ASN195 |
| B | ASP208 |
| B | ADP304 |
| B | HOH402 |
| B | HOH467 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG B 302 |
| Chain | Residue |
| B | ASP208 |
| B | ADP304 |
| B | HOH451 |
| B | HOH452 |
| B | HOH465 |
| site_id | AC5 |
| Number of Residues | 24 |
| Details | BINDING SITE FOR RESIDUE ADP A 303 |
| Chain | Residue |
| A | ASP22 |
| A | GLU24 |
| A | SER27 |
| A | VAL31 |
| A | TYR42 |
| A | LYS44 |
| A | MET90 |
| A | SER91 |
| A | GLU92 |
| A | ALA93 |
| A | LEU97 |
| A | SER194 |
| A | ASN195 |
| A | PHE197 |
| A | ILE207 |
| A | ASP208 |
| A | MG301 |
| A | MG302 |
| A | HOH413 |
| A | HOH423 |
| A | HOH438 |
| A | HOH483 |
| A | HOH491 |
| A | HOH542 |
| site_id | AC6 |
| Number of Residues | 26 |
| Details | BINDING SITE FOR RESIDUE ADP B 304 |
| Chain | Residue |
| B | ASP22 |
| B | GLU24 |
| B | SER27 |
| B | VAL31 |
| B | TYR42 |
| B | LYS44 |
| B | MET90 |
| B | SER91 |
| B | GLU92 |
| B | ALA93 |
| B | LEU97 |
| B | SER194 |
| B | ASN195 |
| B | PHE197 |
| B | ILE207 |
| B | ASP208 |
| B | MG301 |
| B | MG302 |
| B | HOH402 |
| B | HOH439 |
| B | HOH451 |
| B | HOH459 |
| B | HOH465 |
| B | HOH467 |
| B | HOH492 |
| B | HOH520 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000250"}]} |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1l8t |
| Chain | Residue | Details |
| A | LYS44 | |
| A | ASP190 | |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1l8t |
| Chain | Residue | Details |
| B | LYS44 | |
| B | ASP190 | |
| site_id | MCSA1 |
| Number of Residues | 4 |
| Details | M-CSA 640 |
| Chain | Residue | Details |
| A | LYS44 | electrostatic stabiliser, polar interaction |
| A | ASP190 | proton acceptor, proton shuttle (general acid/base) |
| A | ASN195 | metal ligand |
| A | ASP208 | metal ligand |
| site_id | MCSA2 |
| Number of Residues | 4 |
| Details | M-CSA 640 |
| Chain | Residue | Details |
| B | LYS44 | electrostatic stabiliser, polar interaction |
| B | ASP190 | proton acceptor, proton shuttle (general acid/base) |
| B | ASN195 | metal ligand |
| B | ASP208 | metal ligand |
