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: 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 | |
G | HIS66 | |
G | HIS68 | |
G | HIS276 | |
G | ASP327 | |
H | HIS66 | |
A | HIS276 | |
H | HIS68 | |
H | HIS276 | |
H | ASP327 | |
I | HIS66 | |
I | HIS68 | |
I | HIS276 | |
I | ASP327 | |
J | HIS66 | |
J | HIS68 | |
J | HIS276 | |
A | ASP327 | |
J | ASP327 | |
K | HIS66 | |
K | HIS68 | |
K | HIS276 | |
K | ASP327 | |
L | HIS66 | |
L | HIS68 | |
L | HIS276 | |
L | ASP327 | |
B | HIS66 | |
B | HIS68 | |
B | HIS276 | |
B | ASP327 | |
C | HIS66 |
site_id | SWS_FT_FI2 |
Number of Residues | 36 |
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 | |
G | PHE84 | |
A | ASN328 | |
G | ASN328 | |
G | SER331 | |
H | PHE84 | |
H | ASN328 | |
H | SER331 | |
I | PHE84 | |
I | ASN328 | |
I | SER331 | |
J | PHE84 | |
J | ASN328 | |
A | SER331 | |
J | SER331 | |
K | PHE84 | |
K | ASN328 | |
K | SER331 | |
L | PHE84 | |
L | ASN328 | |
L | SER331 | |
B | PHE84 | |
B | ASN328 | |
B | SER331 | |
C | PHE84 | |
C | ASN328 | |
C | SER331 |