4V1X
The structure of the hexameric atrazine chlorohydrolase, AtzA
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0016810 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds |
| A | 0018788 | molecular_function | atrazine chlorohydrolase activity |
| A | 0019381 | biological_process | atrazine catabolic process |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0016810 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds |
| B | 0018788 | molecular_function | atrazine chlorohydrolase activity |
| B | 0019381 | biological_process | atrazine catabolic process |
| B | 0046872 | molecular_function | metal ion binding |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0016787 | molecular_function | hydrolase activity |
| C | 0016810 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds |
| C | 0018788 | molecular_function | atrazine chlorohydrolase activity |
| C | 0019381 | biological_process | atrazine catabolic process |
| C | 0046872 | molecular_function | metal ion binding |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0016787 | molecular_function | hydrolase activity |
| D | 0016810 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds |
| D | 0018788 | molecular_function | atrazine chlorohydrolase activity |
| D | 0019381 | biological_process | atrazine catabolic process |
| D | 0046872 | molecular_function | metal ion binding |
| E | 0005737 | cellular_component | cytoplasm |
| E | 0016787 | molecular_function | hydrolase activity |
| E | 0016810 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds |
| E | 0018788 | molecular_function | atrazine chlorohydrolase activity |
| E | 0019381 | biological_process | atrazine catabolic process |
| E | 0046872 | molecular_function | metal ion binding |
| F | 0005737 | cellular_component | cytoplasm |
| F | 0016787 | molecular_function | hydrolase activity |
| F | 0016810 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds |
| F | 0018788 | molecular_function | atrazine chlorohydrolase activity |
| F | 0019381 | biological_process | atrazine catabolic process |
| F | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE FE A 481 |
| Chain | Residue |
| A | HIS66 |
| A | HIS68 |
| A | HIS243 |
| A | HIS276 |
| A | ASP327 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE FE B 481 |
| Chain | Residue |
| B | ASP327 |
| B | HOH2028 |
| B | HIS66 |
| B | HIS68 |
| B | HIS243 |
| B | HIS276 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE FE C 481 |
| Chain | Residue |
| C | HIS66 |
| C | HIS68 |
| C | HIS243 |
| C | HIS276 |
| C | ASP327 |
| C | HOH2183 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE FE D 481 |
| Chain | Residue |
| D | HIS66 |
| D | HIS68 |
| D | HIS243 |
| D | HIS276 |
| D | ASP327 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE FE E 481 |
| Chain | Residue |
| E | HIS66 |
| E | HIS68 |
| E | HIS243 |
| E | HIS276 |
| E | ASP327 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE FE F 481 |
| Chain | Residue |
| F | HIS66 |
| F | HIS68 |
| F | HIS243 |
| F | HIS276 |
| F | ASP327 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE PEG B 1475 |
| Chain | Residue |
| B | GLU260 |
| B | LYS283 |
| B | HOH2090 |
| B | HOH2126 |
| B | HOH2127 |
| F | GLN83 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PEG D 1475 |
| Chain | Residue |
| B | GLN83 |
| B | LEU171 |
| B | ARG174 |
| D | GLU260 |
| D | LYS283 |
| site_id | AC9 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE PEG C 1475 |
| Chain | Residue |
| C | GLU260 |
| C | LYS283 |
| C | HOH2107 |
| C | HOH2184 |
| C | HOH2185 |
| E | GLN83 |
| E | LEU171 |
| site_id | BC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PEG E 1475 |
| Chain | Residue |
| A | LEU171 |
| A | HOH2034 |
| B | HOH2108 |
| E | GLU260 |
| E | LYS283 |
| site_id | BC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE PEG F 1475 |
| Chain | Residue |
| C | HOH2137 |
| D | GLN83 |
| D | HOH2027 |
| D | HOH2029 |
| F | GLU260 |
| F | LYS283 |
| site_id | BC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE PEG A 1475 |
| Chain | Residue |
| A | GLU260 |
| A | LYS283 |
| A | HOH2160 |
| A | HOH2161 |
| C | GLN83 |
| C | ARG174 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 24 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:25760618, ECO:0007744|PDB:4V1Y |
| Chain | Residue | Details |
| A | HIS66 | |
| C | HIS68 | |
| C | HIS276 | |
| C | ASP327 | |
| D | HIS66 | |
| D | HIS68 | |
| D | HIS276 | |
| D | ASP327 | |
| E | HIS66 | |
| E | HIS68 | |
| E | HIS276 | |
| A | HIS68 | |
| E | ASP327 | |
| F | HIS66 | |
| F | HIS68 | |
| F | HIS276 | |
| F | ASP327 | |
| A | HIS276 | |
| A | ASP327 | |
| B | HIS66 | |
| B | HIS68 | |
| B | HIS276 | |
| B | ASP327 | |
| C | HIS66 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 18 |
| Details | SITE: Major determinant of atrazine specificity => ECO:0000305|PubMed:22768133 |
| Chain | Residue | Details |
| A | PHE84 | |
| D | PHE84 | |
| D | ASN328 | |
| D | SER331 | |
| E | PHE84 | |
| E | ASN328 | |
| E | SER331 | |
| F | PHE84 | |
| F | ASN328 | |
| F | SER331 | |
| A | ASN328 | |
| A | SER331 | |
| B | PHE84 | |
| B | ASN328 | |
| B | SER331 | |
| C | PHE84 | |
| C | ASN328 | |
| C | SER331 |
