6BUN
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 | HOH569 |
| 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 | HOH545 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | binding site for residue CL A 403 |
| Chain | Residue |
| A | ASP266 |
| A | ALA267 |
| A | ASP268 |
| A | ARG309 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | binding site for residue PDO A 404 |
| Chain | Residue |
| A | ASP210 |
| A | LYS211 |
| A | ASP282 |
| A | ASP283 |
| A | HOH540 |
| A | HOH767 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | binding site for residue PDO A 405 |
| Chain | Residue |
| A | ASP317 |
| A | HOH528 |
| A | HOH706 |
| C | HOH586 |
| C | HOH612 |
| D | HOH658 |
| site_id | AC6 |
| Number of Residues | 8 |
| Details | binding site for residue PDO A 406 |
| Chain | Residue |
| A | TRP221 |
| A | GLU301 |
| A | ALA350 |
| A | GLU351 |
| A | ASP356 |
| A | HOH510 |
| A | HOH545 |
| A | HOH620 |
| site_id | AC7 |
| Number of Residues | 7 |
| Details | binding site for residue PDO A 407 |
| Chain | Residue |
| A | GLY53 |
| A | THR56 |
| A | GLN57 |
| A | ARG71 |
| A | HOH539 |
| A | HOH715 |
| A | HOH734 |
| site_id | AC8 |
| Number of Residues | 7 |
| Details | binding site for residue PDO A 408 |
| Chain | Residue |
| A | ASP283 |
| A | ASP291 |
| A | HOH527 |
| A | HOH564 |
| B | LYS3 |
| B | ASP253 |
| B | HOH610 |
| site_id | AC9 |
| Number of Residues | 7 |
| Details | binding site for residue CA A 409 |
| Chain | Residue |
| A | ALA107 |
| A | GLY109 |
| A | SER250 |
| A | HOH519 |
| A | HOH556 |
| A | HOH603 |
| A | HOH830 |
| site_id | AD1 |
| 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 | HOH523 |
| site_id | AD2 |
| 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 | HOH695 |
| site_id | AD3 |
| Number of Residues | 6 |
| Details | binding site for residue CA B 403 |
| Chain | Residue |
| A | HOH666 |
| B | GLU168 |
| B | HOH738 |
| B | HOH757 |
| B | HOH782 |
| C | HOH697 |
| site_id | AD4 |
| Number of Residues | 12 |
| Details | binding site for residue MLI B 404 |
| Chain | Residue |
| B | THR56 |
| B | VAL75 |
| B | PHE80 |
| B | GLU235 |
| B | GLU240 |
| B | PDO406 |
| B | HOH510 |
| B | HOH516 |
| B | HOH520 |
| B | HOH557 |
| B | HOH583 |
| B | HOH605 |
| site_id | AD5 |
| Number of Residues | 6 |
| Details | binding site for residue CL B 405 |
| Chain | Residue |
| B | ASP266 |
| B | ALA267 |
| B | ASP268 |
| B | ARG309 |
| B | HOH615 |
| B | HOH781 |
| site_id | AD6 |
| Number of Residues | 10 |
| Details | binding site for residue PDO B 406 |
| Chain | Residue |
| B | ASP49 |
| B | ARG52 |
| B | LYS161 |
| B | GLY233 |
| B | VAL234 |
| B | GLU235 |
| B | MLI404 |
| B | HOH502 |
| B | HOH510 |
| B | HOH605 |
| site_id | AD7 |
| Number of Residues | 5 |
| Details | binding site for residue PDO B 407 |
| Chain | Residue |
| B | GLU5 |
| B | VAL6 |
| B | ARG366 |
| B | HOH710 |
| B | HOH714 |
| site_id | AD8 |
| 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 | HOH553 |
| site_id | AD9 |
| 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 | HOH705 |
| site_id | AE1 |
| Number of Residues | 2 |
| Details | binding site for residue CL C 403 |
| Chain | Residue |
| C | ASN134 |
| C | HOH609 |
| site_id | AE2 |
| Number of Residues | 7 |
| Details | binding site for residue PDO C 404 |
| Chain | Residue |
| C | PHE50 |
| C | ARG169 |
| C | VAL234 |
| C | HOH622 |
| C | HOH694 |
| D | SER13 |
| D | ASP15 |
| site_id | AE3 |
| Number of Residues | 6 |
| Details | binding site for residue PDO C 405 |
| Chain | Residue |
| C | GLU5 |
| C | VAL6 |
| C | LEU254 |
| C | HOH600 |
| C | HOH627 |
| C | HOH673 |
| site_id | AE4 |
| Number of Residues | 8 |
| Details | binding site for residue PDO C 406 |
| Chain | Residue |
| A | ILE321 |
| A | ALA329 |
| A | HOH572 |
| C | GLU87 |
| C | ILE321 |
| C | ARG325 |
| C | ALA329 |
| C | HOH521 |
| site_id | AE5 |
| Number of Residues | 5 |
| Details | binding site for residue CA C 407 |
| Chain | Residue |
| C | ALA107 |
| C | PRO108 |
| C | GLY109 |
| C | HOH509 |
| C | HOH551 |
| site_id | AE6 |
| Number of Residues | 7 |
| Details | binding site for residue CA C 408 |
| Chain | Residue |
| B | HOH565 |
| B | HOH719 |
| B | HOH774 |
| C | SER319 |
| C | ASN322 |
| C | HOH530 |
| C | HOH574 |
| site_id | AE7 |
| Number of Residues | 7 |
| Details | binding site for residue CA D 401 |
| Chain | Residue |
| D | GLU301 |
| D | ALA350 |
| D | GLN353 |
| D | GLY354 |
| D | PRO355 |
| D | GLY358 |
| D | HOH630 |
| site_id | AE8 |
| Number of Residues | 4 |
| Details | binding site for residue CL D 402 |
| Chain | Residue |
| D | ALA302 |
| D | HIS323 |
| D | THR324 |
| D | HOH529 |
| site_id | AE9 |
| Number of Residues | 6 |
| Details | binding site for residue PDO D 403 |
| Chain | Residue |
| D | ILE207 |
| D | ASN222 |
| D | LEU223 |
| D | TYR224 |
| D | HOH537 |
| D | HOH583 |
| site_id | AF1 |
| Number of Residues | 8 |
| Details | binding site for residue PDO D 404 |
| Chain | Residue |
| D | VAL47 |
| D | ASP49 |
| D | PHE50 |
| D | ARG52 |
| D | HOH504 |
| D | HOH592 |
| D | HOH650 |
| D | HOH658 |
| site_id | AF2 |
| Number of Residues | 7 |
| Details | binding site for residue PDO D 405 |
| Chain | Residue |
| D | GLU5 |
| D | VAL6 |
| D | PHE7 |
| D | LEU254 |
| D | HOH562 |
| D | HOH582 |
| D | HOH640 |
| site_id | AF3 |
| Number of Residues | 5 |
| Details | binding site for residue PDO D 406 |
| Chain | Residue |
| B | GLU87 |
| B | GLY88 |
| B | ALA329 |
| D | ILE321 |
| D | SER326 |
| site_id | AF4 |
| Number of Residues | 4 |
| Details | binding site for residue PDO D 407 |
| Chain | Residue |
| D | ARG52 |
| D | GLY348 |
| D | GLY349 |
| D | HOH512 |
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 |
