6BUP
Crystal structures of cyanuric acid hydrolase from Moorella thermoacetica complexed with cyanuric acid
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0016787 | molecular_function | hydrolase activity |
A | 0016812 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amides |
A | 0018753 | molecular_function | cyanuric acid amidohydrolase activity |
A | 0019381 | biological_process | atrazine catabolic process |
A | 0046872 | molecular_function | metal ion binding |
B | 0016787 | molecular_function | hydrolase activity |
B | 0016812 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amides |
B | 0018753 | molecular_function | cyanuric acid amidohydrolase activity |
B | 0019381 | biological_process | atrazine catabolic process |
B | 0046872 | molecular_function | metal ion binding |
C | 0016787 | molecular_function | hydrolase activity |
C | 0016812 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amides |
C | 0018753 | molecular_function | cyanuric acid amidohydrolase activity |
C | 0019381 | biological_process | atrazine catabolic process |
C | 0046872 | molecular_function | metal ion binding |
D | 0016787 | molecular_function | hydrolase activity |
D | 0016812 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amides |
D | 0018753 | molecular_function | cyanuric acid amidohydrolase activity |
D | 0019381 | biological_process | atrazine catabolic process |
D | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 11 |
Details | binding site for residue MLI A 401 |
Chain | Residue |
A | GLY45 |
A | GLY348 |
A | HOH555 |
A | ARG52 |
A | SER83 |
A | GLY84 |
A | LYS161 |
A | SER231 |
A | ALA232 |
A | ARG328 |
A | SER347 |
site_id | AC2 |
Number of Residues | 7 |
Details | binding site for residue CA A 402 |
Chain | Residue |
A | GLU301 |
A | ALA350 |
A | GLN353 |
A | GLY354 |
A | PRO355 |
A | GLY358 |
A | HOH543 |
site_id | AC3 |
Number of Residues | 7 |
Details | binding site for residue PDO A 403 |
Chain | Residue |
A | ILE321 |
A | ARG325 |
A | ALA329 |
A | HOH505 |
C | ARG325 |
C | ALA329 |
C | HOH555 |
site_id | AC4 |
Number of Residues | 6 |
Details | binding site for residue PDO A 404 |
Chain | Residue |
A | GLU5 |
A | VAL6 |
A | LEU254 |
A | ARG366 |
A | HOH522 |
A | HOH575 |
site_id | AC5 |
Number of Residues | 5 |
Details | binding site for residue PDO A 405 |
Chain | Residue |
A | LYS187 |
A | TYR191 |
A | CYS218 |
A | TRP221 |
A | HOH540 |
site_id | AC6 |
Number of Residues | 4 |
Details | binding site for residue PDO A 406 |
Chain | Residue |
A | HIS156 |
A | HIS258 |
A | ASP276 |
A | HOH503 |
site_id | AC7 |
Number of Residues | 8 |
Details | binding site for residue PEG A 407 |
Chain | Residue |
A | TRP221 |
A | GLU301 |
A | ALA302 |
A | ALA350 |
A | GLU351 |
A | ASP356 |
A | HOH540 |
A | HOH543 |
site_id | AC8 |
Number of Residues | 3 |
Details | binding site for residue PDO A 408 |
Chain | Residue |
A | LYS76 |
A | LYS77 |
A | HOH512 |
site_id | AC9 |
Number of Residues | 12 |
Details | binding site for residue MLI B 401 |
Chain | Residue |
B | GLY45 |
B | ARG52 |
B | SER83 |
B | GLY84 |
B | LYS161 |
B | SER231 |
B | ALA232 |
B | ARG328 |
B | SER347 |
B | GLY348 |
B | WDL402 |
B | HOH535 |
site_id | AD1 |
Number of Residues | 11 |
Details | binding site for residue WDL B 402 |
Chain | Residue |
B | GLY45 |
B | ARG52 |
B | GLY84 |
B | ARG193 |
B | SER231 |
B | ALA232 |
B | ARG328 |
B | SER347 |
B | GLY348 |
B | MLI401 |
B | HOH535 |
site_id | AD2 |
Number of Residues | 7 |
Details | binding site for residue CA B 403 |
Chain | Residue |
B | GLU301 |
B | ALA350 |
B | GLN353 |
B | GLY354 |
B | PRO355 |
B | GLY358 |
B | HOH581 |
site_id | AD3 |
Number of Residues | 5 |
Details | binding site for residue PDO B 404 |
Chain | Residue |
B | GLU5 |
B | VAL6 |
B | ARG366 |
B | HOH573 |
B | HOH609 |
site_id | AD4 |
Number of Residues | 8 |
Details | binding site for residue PDO B 405 |
Chain | Residue |
B | TRP221 |
B | GLU301 |
B | SER304 |
B | ALA350 |
B | GLU351 |
B | ASP356 |
B | HOH503 |
B | HOH581 |
site_id | AD5 |
Number of Residues | 5 |
Details | binding site for residue PDO B 406 |
Chain | Residue |
B | ILE207 |
B | ASN222 |
B | LEU223 |
B | TYR224 |
B | HOH694 |
site_id | AD6 |
Number of Residues | 12 |
Details | binding site for residue MLI C 401 |
Chain | Residue |
C | GLY45 |
C | ARG52 |
C | SER83 |
C | GLY84 |
C | LYS161 |
C | SER231 |
C | ALA232 |
C | ARG328 |
C | SER347 |
C | GLY348 |
C | WDL402 |
C | HOH503 |
site_id | AD7 |
Number of Residues | 14 |
Details | binding site for residue WDL C 402 |
Chain | Residue |
C | GLY45 |
C | ARG52 |
C | SER83 |
C | GLY84 |
C | LYS161 |
C | MET189 |
C | ARG193 |
C | SER231 |
C | ALA232 |
C | ARG328 |
C | SER347 |
C | GLY348 |
C | MLI401 |
C | HOH503 |
site_id | AD8 |
Number of Residues | 7 |
Details | binding site for residue CA C 403 |
Chain | Residue |
C | GLU301 |
C | ALA350 |
C | GLN353 |
C | GLY354 |
C | PRO355 |
C | GLY358 |
C | HOH596 |
site_id | AD9 |
Number of Residues | 7 |
Details | binding site for residue PDO C 404 |
Chain | Residue |
B | TYR186 |
B | HOH501 |
B | HOH607 |
C | LEU316 |
C | ASP318 |
C | SER319 |
C | HOH514 |
site_id | AE1 |
Number of Residues | 8 |
Details | binding site for residue WDL C 405 |
Chain | Residue |
B | SER304 |
B | LEU316 |
C | ALA167 |
C | ILE170 |
C | ASN183 |
C | THR185 |
C | HOH534 |
C | HOH572 |
site_id | AE2 |
Number of Residues | 6 |
Details | binding site for residue PDO C 406 |
Chain | Residue |
C | TRP221 |
C | GLU301 |
C | GLU351 |
C | ASP356 |
C | HOH506 |
C | HOH596 |
site_id | AE3 |
Number of Residues | 5 |
Details | binding site for residue PDO C 407 |
Chain | Residue |
C | GLU5 |
C | VAL6 |
C | LEU254 |
C | HOH507 |
C | HOH654 |
site_id | AE4 |
Number of Residues | 8 |
Details | binding site for residue MLI D 401 |
Chain | Residue |
D | GLY45 |
D | ARG52 |
D | SER83 |
D | GLY84 |
D | ARG328 |
D | SER347 |
D | GLY348 |
D | HOH503 |
site_id | AE5 |
Number of Residues | 7 |
Details | binding site for residue CA D 402 |
Chain | Residue |
D | GLU301 |
D | ALA350 |
D | GLN353 |
D | GLY354 |
D | PRO355 |
D | GLY358 |
D | HOH584 |
site_id | AE6 |
Number of Residues | 3 |
Details | binding site for residue CL D 404 |
Chain | Residue |
D | VAL6 |
D | HOH507 |
D | HOH627 |
site_id | AE7 |
Number of Residues | 3 |
Details | binding site for residue CL D 405 |
Chain | Residue |
D | TRP221 |
D | GLU301 |
D | HOH584 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 4 |
Details | ACT_SITE: ACT_SITE => ECO:0000255|HAMAP-Rule:MF_01989 |
Chain | Residue | Details |
A | LYS161 | |
B | LYS161 | |
C | LYS161 | |
D | LYS161 |
site_id | SWS_FT_FI2 |
Number of Residues | 4 |
Details | ACT_SITE: Nucleophile => ECO:0000255|HAMAP-Rule:MF_01989 |
Chain | Residue | Details |
A | SER231 | |
B | SER231 | |
C | SER231 | |
D | SER231 |
site_id | SWS_FT_FI3 |
Number of Residues | 48 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01989 |
Chain | Residue | Details |
A | ARG52 | |
A | GLY359 | |
A | PRO360 | |
A | VAL363 | |
B | ARG52 | |
B | SER83 | |
B | ARG193 | |
B | SER231 | |
B | GLY306 | |
B | ALA333 | |
B | HIS352 | |
A | SER83 | |
B | PRO355 | |
B | GLY358 | |
B | GLY359 | |
B | PRO360 | |
B | VAL363 | |
C | ARG52 | |
C | SER83 | |
C | ARG193 | |
C | SER231 | |
C | GLY306 | |
A | ARG193 | |
C | ALA333 | |
C | HIS352 | |
C | PRO355 | |
C | GLY358 | |
C | GLY359 | |
C | PRO360 | |
C | VAL363 | |
D | ARG52 | |
D | SER83 | |
D | ARG193 | |
A | SER231 | |
D | SER231 | |
D | GLY306 | |
D | ALA333 | |
D | HIS352 | |
D | PRO355 | |
D | GLY358 | |
D | GLY359 | |
D | PRO360 | |
D | VAL363 | |
A | GLY306 | |
A | ALA333 | |
A | HIS352 | |
A | PRO355 | |
A | GLY358 |
site_id | SWS_FT_FI4 |
Number of Residues | 4 |
Details | SITE: Important for substrate specificity => ECO:0000255|HAMAP-Rule:MF_01989 |
Chain | Residue | Details |
A | ALA329 | |
B | ALA329 | |
C | ALA329 | |
D | ALA329 |