6FZB
AadA in complex with ATP, magnesium and streptomycin
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0005524 | molecular_function | ATP binding |
| A | 0009012 | molecular_function | aminoglycoside 3''-adenylyltransferase activity |
| A | 0016740 | molecular_function | transferase activity |
| A | 0016779 | molecular_function | nucleotidyltransferase activity |
| A | 0046677 | biological_process | response to antibiotic |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0070566 | molecular_function | adenylyltransferase activity |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0005524 | molecular_function | ATP binding |
| B | 0009012 | molecular_function | aminoglycoside 3''-adenylyltransferase activity |
| B | 0016740 | molecular_function | transferase activity |
| B | 0016779 | molecular_function | nucleotidyltransferase activity |
| B | 0046677 | biological_process | response to antibiotic |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0070566 | molecular_function | adenylyltransferase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 10 |
| Details | binding site for residue SRY A 301 |
| Chain | Residue |
| A | GLU87 |
| A | HOH411 |
| A | TRP112 |
| A | ASP130 |
| A | TRP173 |
| A | ALA177 |
| A | ASP178 |
| A | ASP182 |
| A | HIS185 |
| A | ATP304 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | binding site for residue MG A 302 |
| Chain | Residue |
| A | ASP47 |
| A | ASP49 |
| A | MG303 |
| A | ATP304 |
| A | HOH407 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | binding site for residue MG A 303 |
| Chain | Residue |
| A | ASP47 |
| A | ASP49 |
| A | GLU87 |
| A | MG302 |
| A | ATP304 |
| A | HOH425 |
| site_id | AC4 |
| Number of Residues | 25 |
| Details | binding site for residue ATP A 304 |
| Chain | Residue |
| A | SER36 |
| A | GLY41 |
| A | SER46 |
| A | ASP47 |
| A | ASP49 |
| A | ASP130 |
| A | LEU133 |
| A | LEU134 |
| A | GLN137 |
| A | ARG192 |
| A | ILE193 |
| A | THR196 |
| A | PHE202 |
| A | LYS205 |
| A | TYR231 |
| A | SRY301 |
| A | MG302 |
| A | MG303 |
| A | HOH407 |
| A | HOH422 |
| A | HOH448 |
| A | HOH457 |
| A | HOH460 |
| A | HOH480 |
| A | HOH483 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | binding site for residue CL A 305 |
| Chain | Residue |
| B | GLY41 |
| B | LEU42 |
| B | PHE252 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | binding site for residue CL A 306 |
| Chain | Residue |
| A | GLY41 |
| A | LEU42 |
| A | PHE252 |
| A | HOH440 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | binding site for residue PEG A 307 |
| Chain | Residue |
| A | GLU151 |
| A | ARG152 |
| A | PHE154 |
| A | THR155 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | binding site for residue PEG A 308 |
| Chain | Residue |
| B | GLU151 |
| B | ARG152 |
| B | LEU153 |
| B | THR155 |
| site_id | AC9 |
| Number of Residues | 10 |
| Details | binding site for residue SRY B 301 |
| Chain | Residue |
| B | GLU87 |
| B | TRP112 |
| B | ASP130 |
| B | TRP173 |
| B | ALA177 |
| B | ASP178 |
| B | ASP182 |
| B | HIS185 |
| B | ATP304 |
| B | HOH439 |
| site_id | AD1 |
| Number of Residues | 5 |
| Details | binding site for residue MG B 302 |
| Chain | Residue |
| B | ASP47 |
| B | ASP49 |
| B | MG303 |
| B | ATP304 |
| B | HOH405 |
| site_id | AD2 |
| Number of Residues | 5 |
| Details | binding site for residue MG B 303 |
| Chain | Residue |
| B | ASP47 |
| B | ASP49 |
| B | GLU87 |
| B | MG302 |
| B | ATP304 |
| site_id | AD3 |
| Number of Residues | 26 |
| Details | binding site for residue ATP B 304 |
| Chain | Residue |
| B | MG303 |
| B | HOH405 |
| B | HOH422 |
| B | HOH438 |
| B | HOH447 |
| B | HOH459 |
| B | HOH470 |
| B | HOH472 |
| B | SER36 |
| B | GLY41 |
| B | SER46 |
| B | ASP47 |
| B | ASP49 |
| B | ASP130 |
| B | LEU133 |
| B | LEU134 |
| B | GLN137 |
| B | LEU166 |
| B | ARG192 |
| B | ILE193 |
| B | THR196 |
| B | PHE202 |
| B | LYS205 |
| B | TYR231 |
| B | SRY301 |
| B | MG302 |
| site_id | AD4 |
| Number of Residues | 13 |
| Details | binding site for residue GOL B 305 |
| Chain | Residue |
| A | ALA15 |
| A | ALA15 |
| A | ARG18 |
| A | ARG18 |
| A | ARG22 |
| A | ARG22 |
| B | ALA15 |
| B | ALA15 |
| B | ARG18 |
| B | ARG18 |
| B | LEU19 |
| B | ARG22 |
| B | ARG22 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 208 |
| Details | Region: {"description":"Helical domain","evidences":[{"source":"PubMed","id":"26527143","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"26527143","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"29871922","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 16 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"29871922","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5G4A","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5LPA","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5LUH","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6FZB","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 10 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"29871922","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5LPA","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5LUH","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6FZB","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"29871922","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5LPA","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5LUH","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
