6BUO
Crystal structures of cyanuric acid hydrolase from Moorella thermoacetica
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 | HOH532 |
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 | HOH527 |
site_id | AC3 |
Number of Residues | 7 |
Details | binding site for residue PDO A 403 |
Chain | Residue |
A | GLU5 |
A | VAL6 |
A | LEU254 |
A | ARG366 |
A | HOH529 |
A | HOH669 |
A | HOH689 |
site_id | AC4 |
Number of Residues | 8 |
Details | binding site for residue PDO A 404 |
Chain | Residue |
A | TRP221 |
A | GLU301 |
A | ALA302 |
A | ALA350 |
A | GLU351 |
A | ASP356 |
A | HOH527 |
A | HOH609 |
site_id | AC5 |
Number of Residues | 4 |
Details | binding site for residue PDO A 405 |
Chain | Residue |
A | LYS76 |
A | LYS77 |
A | HOH570 |
A | HOH666 |
site_id | AC6 |
Number of Residues | 5 |
Details | binding site for residue PDO A 406 |
Chain | Residue |
A | ARG271 |
A | ILE279 |
A | ARG280 |
A | SER281 |
A | ASP282 |
site_id | AC7 |
Number of Residues | 7 |
Details | binding site for residue PDO A 407 |
Chain | Residue |
A | PRO124 |
A | LEU164 |
A | ARG169 |
A | LEU237 |
A | HOH520 |
A | HOH574 |
A | HOH579 |
site_id | AC8 |
Number of Residues | 6 |
Details | binding site for residue PDO A 408 |
Chain | Residue |
A | GLU131 |
A | ASN134 |
A | HOH561 |
B | GLU135 |
B | ARG138 |
B | HOH507 |
site_id | AC9 |
Number of Residues | 6 |
Details | binding site for residue PDO A 409 |
Chain | Residue |
A | VAL75 |
A | GLU235 |
A | GLU240 |
A | HOH525 |
A | HOH627 |
A | HOH718 |
site_id | AD1 |
Number of Residues | 5 |
Details | binding site for residue PDO A 410 |
Chain | Residue |
A | ASP15 |
A | ASP16 |
A | HOH543 |
A | HOH554 |
A | HOH723 |
site_id | AD2 |
Number of Residues | 9 |
Details | binding site for residue PDO A 411 |
Chain | Residue |
A | THR166 |
A | ALA167 |
A | GLU168 |
A | HOH502 |
A | HOH636 |
B | ALA12 |
D | ARG312 |
D | ASP317 |
D | HOH620 |
site_id | AD3 |
Number of Residues | 3 |
Details | binding site for residue PDO A 412 |
Chain | Residue |
A | ARG309 |
A | ARG311 |
C | GLY340 |
site_id | AD4 |
Number of Residues | 11 |
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 | HOH536 |
site_id | AD5 |
Number of Residues | 7 |
Details | binding site for residue CA B 402 |
Chain | Residue |
B | GLU301 |
B | ALA350 |
B | GLN353 |
B | GLY354 |
B | PRO355 |
B | GLY358 |
B | HOH543 |
site_id | AD6 |
Number of Residues | 7 |
Details | binding site for residue PDO B 403 |
Chain | Residue |
B | ARG366 |
B | HOH636 |
B | HOH653 |
B | HOH664 |
B | GLU5 |
B | VAL6 |
B | LEU254 |
site_id | AD7 |
Number of Residues | 6 |
Details | binding site for residue PDO B 404 |
Chain | Residue |
B | ARG271 |
B | LEU274 |
B | LYS275 |
B | ILE279 |
B | ASP282 |
B | MET290 |
site_id | AD8 |
Number of Residues | 7 |
Details | binding site for residue PDO B 405 |
Chain | Residue |
B | TRP221 |
B | GLU301 |
B | GLU351 |
B | ASP356 |
B | PDO409 |
B | HOH543 |
B | HOH635 |
site_id | AD9 |
Number of Residues | 5 |
Details | binding site for residue PDO B 406 |
Chain | Residue |
B | ARG309 |
B | ARG311 |
D | GLY340 |
D | ASP341 |
D | HOH659 |
site_id | AE1 |
Number of Residues | 9 |
Details | binding site for residue PDO B 407 |
Chain | Residue |
B | TYR186 |
B | ASN322 |
B | HOH514 |
B | HOH616 |
B | HOH712 |
C | SER319 |
C | HOH526 |
C | HOH532 |
C | HOH653 |
site_id | AE2 |
Number of Residues | 7 |
Details | binding site for residue PDO B 408 |
Chain | Residue |
B | GLU87 |
B | ILE321 |
B | ALA329 |
B | HOH505 |
B | HOH506 |
D | GLU87 |
D | ILE321 |
site_id | AE3 |
Number of Residues | 9 |
Details | binding site for residue PDO B 409 |
Chain | Residue |
B | TYR186 |
B | LYS187 |
B | ALA190 |
B | HIS323 |
B | GLU351 |
B | PDO405 |
B | HOH520 |
B | HOH651 |
B | HOH720 |
site_id | AE4 |
Number of Residues | 3 |
Details | binding site for residue PDO B 410 |
Chain | Residue |
B | ASN222 |
B | LEU223 |
B | TYR224 |
site_id | AE5 |
Number of Residues | 5 |
Details | binding site for residue PDO B 411 |
Chain | Residue |
B | ILE17 |
B | TYR62 |
B | HOH508 |
B | HOH547 |
B | HOH590 |
site_id | AE6 |
Number of Residues | 11 |
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 | HOH523 |
site_id | AE7 |
Number of Residues | 7 |
Details | binding site for residue CA C 402 |
Chain | Residue |
C | GLU301 |
C | ALA350 |
C | GLN353 |
C | GLY354 |
C | PRO355 |
C | GLY358 |
C | PDO405 |
site_id | AE8 |
Number of Residues | 6 |
Details | binding site for residue PDO C 403 |
Chain | Residue |
C | GLU5 |
C | VAL6 |
C | PHE7 |
C | LEU254 |
C | HOH597 |
C | HOH674 |
site_id | AE9 |
Number of Residues | 9 |
Details | binding site for residue PDO C 404 |
Chain | Residue |
A | GLU87 |
A | ILE321 |
A | SER326 |
A | HOH549 |
C | GLU87 |
C | ILE321 |
C | SER326 |
C | ALA329 |
C | HOH501 |
site_id | AF1 |
Number of Residues | 8 |
Details | binding site for residue PDO C 405 |
Chain | Residue |
C | TRP221 |
C | GLU301 |
C | ALA350 |
C | GLU351 |
C | HIS352 |
C | ASP356 |
C | CA402 |
C | HOH566 |
site_id | AF2 |
Number of Residues | 3 |
Details | binding site for residue PDO C 406 |
Chain | Residue |
C | ALA117 |
C | PHE118 |
C | GLU142 |
site_id | AF3 |
Number of Residues | 2 |
Details | binding site for residue PDO C 407 |
Chain | Residue |
C | ILE279 |
C | ASP282 |
site_id | AF4 |
Number of Residues | 11 |
Details | binding site for residue MLI D 401 |
Chain | Residue |
D | GLY45 |
D | ARG52 |
D | SER83 |
D | GLY84 |
D | LYS161 |
D | SER231 |
D | ALA232 |
D | ARG328 |
D | SER347 |
D | GLY348 |
D | HOH561 |
site_id | AF5 |
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 | HOH615 |
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 |