6CWJ
Crystal structures of cyanuric acid hydrolase from Moorella thermoacetica complexed with 1,3-Acetone Dicarboxylic Acid
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| 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 | 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 | 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 | 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 | 10 |
| Details | binding site for residue MLI A 401 |
| Chain | Residue |
| A | GLY45 |
| A | GLY343 |
| A | ARG52 |
| A | SER83 |
| A | GLY84 |
| A | LYS161 |
| A | SER231 |
| A | ALA232 |
| A | ARG323 |
| A | SER342 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | binding site for residue CA A 402 |
| Chain | Residue |
| A | GLU296 |
| A | ALA345 |
| A | GLN348 |
| A | GLY349 |
| A | PRO350 |
| A | GLY353 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | binding site for residue ACT A 403 |
| Chain | Residue |
| A | ASP313 |
| A | SER314 |
| D | TYR186 |
| D | ASN317 |
| site_id | AC4 |
| Number of Residues | 8 |
| Details | binding site for residue ACT A 404 |
| Chain | Residue |
| A | SER314 |
| A | ASN317 |
| A | HOH515 |
| A | HOH582 |
| D | ASP313 |
| D | SER314 |
| D | ASP315 |
| D | ASN317 |
| site_id | AC5 |
| Number of Residues | 12 |
| Details | binding site for residue 6JN B 401 |
| Chain | Residue |
| B | GLY45 |
| B | ARG52 |
| B | SER83 |
| B | GLY84 |
| B | LYS161 |
| B | MET189 |
| B | ARG193 |
| B | SER231 |
| B | ALA232 |
| B | ARG323 |
| B | SER342 |
| B | GLY343 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | binding site for residue CA B 402 |
| Chain | Residue |
| B | GLU296 |
| B | ALA345 |
| B | GLN348 |
| B | GLY349 |
| B | PRO350 |
| B | GLY353 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | binding site for residue PDO B 403 |
| Chain | Residue |
| B | ALA190 |
| B | GLU296 |
| B | ALA297 |
| B | GLU346 |
| B | ASP351 |
| site_id | AC8 |
| Number of Residues | 12 |
| Details | binding site for residue 6JN C 401 |
| Chain | Residue |
| C | GLY45 |
| C | ARG52 |
| C | SER83 |
| C | GLY84 |
| C | LYS161 |
| C | MET189 |
| C | ARG193 |
| C | SER231 |
| C | ALA232 |
| C | ARG323 |
| C | SER342 |
| C | GLY343 |
| site_id | AC9 |
| Number of Residues | 6 |
| Details | binding site for residue CA C 402 |
| Chain | Residue |
| C | GLU296 |
| C | ALA345 |
| C | GLN348 |
| C | GLY349 |
| C | PRO350 |
| C | GLY353 |
| site_id | AD1 |
| Number of Residues | 5 |
| Details | binding site for residue ACT D 401 |
| Chain | Residue |
| B | ILE316 |
| B | SER321 |
| B | ALA324 |
| D | GLU87 |
| D | ILE316 |
| site_id | AD2 |
| Number of Residues | 12 |
| Details | binding site for residue 6JN D 402 |
| Chain | Residue |
| D | GLY45 |
| D | ARG52 |
| D | SER83 |
| D | GLY84 |
| D | LYS161 |
| D | MET189 |
| D | ARG193 |
| D | SER231 |
| D | ALA232 |
| D | ARG323 |
| D | SER342 |
| D | GLY343 |
| site_id | AD3 |
| Number of Residues | 6 |
| Details | binding site for residue CA D 403 |
| Chain | Residue |
| D | GLU296 |
| D | ALA345 |
| D | GLN348 |
| D | GLY349 |
| D | PRO350 |
| D | GLY353 |
| site_id | AD4 |
| Number of Residues | 5 |
| Details | binding site for residue ACT D 404 |
| Chain | Residue |
| A | ASP312 |
| D | ALA167 |
| D | GLU168 |
| D | HOH537 |
| D | HOH551 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 412 |
| Details | Region: {"description":"RU A","evidences":[{"source":"HAMAP-Rule","id":"MF_01989","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 548 |
| Details | Region: {"description":"RU B","evidences":[{"source":"HAMAP-Rule","id":"MF_01989","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | Active site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01989","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | Active site: {"description":"Nucleophile","evidences":[{"source":"HAMAP-Rule","id":"MF_01989","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 48 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01989","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 4 |
| Details | Site: {"description":"Important for substrate specificity","evidences":[{"source":"HAMAP-Rule","id":"MF_01989","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
