4V1Y
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 |
| G | 0005737 | cellular_component | cytoplasm |
| G | 0016787 | molecular_function | hydrolase activity |
| G | 0016810 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds |
| G | 0018788 | molecular_function | atrazine chlorohydrolase activity |
| G | 0019381 | biological_process | atrazine catabolic process |
| G | 0046872 | molecular_function | metal ion binding |
| H | 0005737 | cellular_component | cytoplasm |
| H | 0016787 | molecular_function | hydrolase activity |
| H | 0016810 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds |
| H | 0018788 | molecular_function | atrazine chlorohydrolase activity |
| H | 0019381 | biological_process | atrazine catabolic process |
| H | 0046872 | molecular_function | metal ion binding |
| I | 0005737 | cellular_component | cytoplasm |
| I | 0016787 | molecular_function | hydrolase activity |
| I | 0016810 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds |
| I | 0018788 | molecular_function | atrazine chlorohydrolase activity |
| I | 0019381 | biological_process | atrazine catabolic process |
| I | 0046872 | molecular_function | metal ion binding |
| J | 0005737 | cellular_component | cytoplasm |
| J | 0016787 | molecular_function | hydrolase activity |
| J | 0016810 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds |
| J | 0018788 | molecular_function | atrazine chlorohydrolase activity |
| J | 0019381 | biological_process | atrazine catabolic process |
| J | 0046872 | molecular_function | metal ion binding |
| K | 0005737 | cellular_component | cytoplasm |
| K | 0016787 | molecular_function | hydrolase activity |
| K | 0016810 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds |
| K | 0018788 | molecular_function | atrazine chlorohydrolase activity |
| K | 0019381 | biological_process | atrazine catabolic process |
| K | 0046872 | molecular_function | metal ion binding |
| L | 0005737 | cellular_component | cytoplasm |
| L | 0016787 | molecular_function | hydrolase activity |
| L | 0016810 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds |
| L | 0018788 | molecular_function | atrazine chlorohydrolase activity |
| L | 0019381 | biological_process | atrazine catabolic process |
| L | 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 | 5 |
| Details | BINDING SITE FOR RESIDUE FE B 481 |
| Chain | Residue |
| B | ASP327 |
| B | HIS66 |
| B | HIS68 |
| B | HIS243 |
| B | HIS276 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE FE C 481 |
| Chain | Residue |
| C | HIS66 |
| C | HIS68 |
| C | HIS243 |
| C | HIS276 |
| C | ASP327 |
| 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 | 5 |
| Details | BINDING SITE FOR RESIDUE FE G 481 |
| Chain | Residue |
| G | HIS66 |
| G | HIS68 |
| G | HIS243 |
| G | HIS276 |
| G | ASP327 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE FE H 481 |
| Chain | Residue |
| H | HIS66 |
| H | HIS68 |
| H | HIS243 |
| H | HIS276 |
| H | ASP327 |
| site_id | AC9 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE FE I 481 |
| Chain | Residue |
| I | HIS66 |
| I | HIS68 |
| I | HIS243 |
| I | HIS276 |
| I | ASP327 |
| site_id | BC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE FE J 481 |
| Chain | Residue |
| J | HIS66 |
| J | HIS68 |
| J | HIS243 |
| J | HIS276 |
| J | ASP327 |
| site_id | BC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE FE K 481 |
| Chain | Residue |
| K | HIS66 |
| K | HIS68 |
| K | HIS243 |
| K | HIS276 |
| K | ASP327 |
| site_id | BC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE FE L 481 |
| Chain | Residue |
| L | HIS66 |
| L | HIS68 |
| L | HIS243 |
| L | HIS276 |
| L | ASP327 |
| site_id | BC4 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE EDO L 1475 |
| Chain | Residue |
| L | ARG19 |
| site_id | BC5 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE EDO F 1475 |
| Chain | Residue |
| F | ARG19 |
| F | LEU36 |
| site_id | BC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO C 1475 |
| Chain | Residue |
| C | ARG282 |
| C | GLU314 |
| C | ARG318 |
| F | ARG282 |
| F | GLU314 |
| F | ARG318 |
| site_id | BC7 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE EDO J 1475 |
| Chain | Residue |
| J | GLU260 |
| J | LYS283 |
| site_id | BC8 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO H 1475 |
| Chain | Residue |
| H | GLU260 |
| H | LYS283 |
| L | HOH2008 |
| site_id | BC9 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE EDO G 1475 |
| Chain | Residue |
| G | GLU260 |
| G | LYS283 |
| site_id | CC1 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE EDO E 1475 |
| Chain | Residue |
| E | GLU260 |
| E | LYS283 |
| site_id | CC2 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE EDO A 1475 |
| Chain | Residue |
| A | LYS283 |
| site_id | CC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO A 1476 |
| Chain | Residue |
| A | ARG282 |
| A | GLU314 |
| A | ARG318 |
| D | ARG282 |
| D | GLU314 |
| D | ARG318 |
| site_id | CC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO L 1476 |
| Chain | Residue |
| I | ARG282 |
| I | GLU314 |
| I | ARG318 |
| L | ARG282 |
| L | GLU314 |
| L | ARG318 |
| site_id | CC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO J 1476 |
| Chain | Residue |
| G | ARG282 |
| G | GLU314 |
| G | ARG318 |
| J | ARG282 |
| J | GLU314 |
| J | ARG318 |
| site_id | CC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO B 1475 |
| Chain | Residue |
| B | ARG318 |
| E | ARG282 |
| E | GLU314 |
| E | ARG318 |
| B | ARG282 |
| B | GLU314 |
| site_id | CC7 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CL H 1476 |
| Chain | Residue |
| H | ARG318 |
| K | ARG318 |
| site_id | CC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PEG B 1476 |
| Chain | Residue |
| B | GLU260 |
| B | LYS283 |
| B | ARG290 |
| E | ASP356 |
| F | ARG174 |
| site_id | CC9 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PEG C 1476 |
| Chain | Residue |
| C | GLU260 |
| C | LYS283 |
| C | HOH2007 |
| E | TYR167 |
| E | ARG174 |
| site_id | DC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE PEG I 1475 |
| Chain | Residue |
| I | GLU260 |
| I | LYS283 |
| I | LEU287 |
| I | ARG290 |
| K | ARG174 |
| L | ASP356 |
| site_id | DC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PEG F 1476 |
| Chain | Residue |
| C | HOH2011 |
| D | GLN83 |
| D | ARG174 |
| F | GLU260 |
| F | LYS283 |
| site_id | DC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE PEG K 1475 |
| Chain | Residue |
| G | ARG174 |
| H | ASP356 |
| K | GLU260 |
| K | GLU263 |
| K | LYS283 |
| K | ARG290 |
| site_id | DC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PEG D 1475 |
| Chain | Residue |
| A | ASP356 |
| B | ARG174 |
| D | LYS283 |
| D | LEU287 |
| D | ARG290 |
| site_id | DC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PEG L 1477 |
| Chain | Residue |
| I | ASP356 |
| J | ARG174 |
| L | GLU260 |
| L | LYS283 |
| L | ARG290 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 48 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"25760618","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4V1Y","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 36 |
| Details | Site: {"description":"Major determinant of atrazine specificity","evidences":[{"source":"PubMed","id":"22768133","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
