6BUR
Crystal structures of cyanuric acid hydrolase from Moorella thermoacetica complexed with barbituric 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 | 13 |
| Details | binding site for residue BR8 A 401 |
| Chain | Residue |
| A | GLY45 |
| A | ARG328 |
| A | SER347 |
| A | GLY348 |
| A | MLI402 |
| A | ARG52 |
| A | SER83 |
| A | GLY84 |
| A | LYS161 |
| A | MET189 |
| A | ARG193 |
| A | SER231 |
| A | ALA232 |
| site_id | AC2 |
| Number of Residues | 12 |
| Details | binding site for residue MLI A 402 |
| Chain | Residue |
| A | GLY45 |
| A | ARG52 |
| A | SER83 |
| A | GLY84 |
| A | LYS161 |
| A | MET189 |
| A | SER231 |
| A | ALA232 |
| A | ARG328 |
| A | SER347 |
| A | GLY348 |
| A | BR8401 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | binding site for residue CA A 403 |
| Chain | Residue |
| A | GLU301 |
| A | ALA350 |
| A | GLN353 |
| A | GLY354 |
| A | PRO355 |
| A | GLY358 |
| A | HOH610 |
| site_id | AC4 |
| Number of Residues | 12 |
| Details | binding site for residue BR8 B 401 |
| Chain | Residue |
| B | GLY45 |
| B | ARG52 |
| B | SER83 |
| B | GLY84 |
| B | LYS161 |
| B | MET189 |
| B | ARG193 |
| B | SER231 |
| B | ALA232 |
| B | ARG328 |
| B | SER347 |
| B | GLY348 |
| site_id | AC5 |
| 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 | HOH580 |
| site_id | AC6 |
| Number of Residues | 11 |
| Details | binding site for residue BR8 C 401 |
| Chain | Residue |
| C | GLY45 |
| C | ARG52 |
| C | SER83 |
| C | GLY84 |
| C | MET189 |
| C | ARG193 |
| C | SER231 |
| C | ALA232 |
| C | ARG328 |
| C | SER347 |
| C | GLY348 |
| site_id | AC7 |
| 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 | HOH593 |
| site_id | AC8 |
| Number of Residues | 11 |
| Details | binding site for residue BR8 D 401 |
| Chain | Residue |
| D | GLY45 |
| D | ARG52 |
| D | SER83 |
| D | GLY84 |
| D | MET189 |
| D | ARG193 |
| D | SER231 |
| D | ALA232 |
| D | ARG328 |
| D | SER347 |
| D | GLY348 |
| site_id | AC9 |
| 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 | HOH546 |
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 |
