1KAN
MOLECULAR STRUCTURE OF KANAMYCIN NUCLEOTIDYLTRANSFERASE DETERMINED TO 3.0-ANGSTROMS RESOLUTION
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0005524 | molecular_function | ATP binding |
| A | 0016740 | molecular_function | transferase activity |
| A | 0016779 | molecular_function | nucleotidyltransferase activity |
| A | 0046677 | biological_process | response to antibiotic |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0005524 | molecular_function | ATP binding |
| B | 0016740 | molecular_function | transferase activity |
| B | 0016779 | molecular_function | nucleotidyltransferase activity |
| B | 0046677 | biological_process | response to antibiotic |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 252 |
| Details | Region: {"description":"N-terminal domain","evidences":[{"source":"PubMed","id":"7577914","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8218273","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 226 |
| Details | Region: {"description":"C-terminal domain","evidences":[{"source":"PubMed","id":"7577914","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8218273","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"7577914","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"7577914","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"1KNY","evidenceCode":"ECO:0000312"},{"source":"PDB","id":"6P06","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"38250052","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6NML","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6NMM","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6NMN","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"21040710","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6UN8","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PDB","id":"6UN8","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"7577914","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1KNY","evidenceCode":"ECO:0000312"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"38250052","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6NMK","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6NML","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6NMN","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6P01","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6P04","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6UN8","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI10 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"7577914","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"1KNY","evidenceCode":"ECO:0000312"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1kny |
| Chain | Residue | Details |
| A | GLU145 | |
| A | LYS149 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1kny |
| Chain | Residue | Details |
| B | GLU145 | |
| B | LYS149 |
| site_id | MCSA1 |
| Number of Residues | 4 |
| Details | M-CSA 647 |
| Chain | Residue | Details |
| A | ASP50 | metal ligand |
| A | GLU52 | metal ligand |
| A | GLU145 | activator, proton acceptor, proton donor |
| A | LYS149 | electrostatic stabiliser, polar interaction |
| site_id | MCSA2 |
| Number of Residues | 4 |
| Details | M-CSA 647 |
| Chain | Residue | Details |
| B | ASP50 | metal ligand |
| B | GLU52 | metal ligand |
| B | GLU145 | activator, proton acceptor, proton donor |
| B | LYS149 | electrostatic stabiliser, polar interaction |
