4LFY
Crystal structure of a dihydroorotase from Burkholderia cenocepacia J2315
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004151 | molecular_function | dihydroorotase activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0006207 | biological_process | 'de novo' pyrimidine nucleobase biosynthetic process |
| A | 0006221 | biological_process | pyrimidine nucleotide biosynthetic process |
| A | 0008270 | molecular_function | zinc ion binding |
| A | 0009220 | biological_process | pyrimidine ribonucleotide biosynthetic process |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0016812 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amides |
| A | 0019856 | biological_process | pyrimidine nucleobase biosynthetic process |
| A | 0044205 | biological_process | 'de novo' UMP biosynthetic process |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0004151 | molecular_function | dihydroorotase activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0006207 | biological_process | 'de novo' pyrimidine nucleobase biosynthetic process |
| B | 0006221 | biological_process | pyrimidine nucleotide biosynthetic process |
| B | 0008270 | molecular_function | zinc ion binding |
| B | 0009220 | biological_process | pyrimidine ribonucleotide biosynthetic process |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0016812 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amides |
| B | 0019856 | biological_process | pyrimidine nucleobase biosynthetic process |
| B | 0044205 | biological_process | 'de novo' UMP biosynthetic process |
| B | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE ZN A 401 |
| Chain | Residue |
| A | HIS31 |
| A | HIS33 |
| A | KCX117 |
| A | ASP268 |
| A | ZN402 |
| A | HOH656 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN A 402 |
| Chain | Residue |
| A | ZN401 |
| A | HOH656 |
| A | KCX117 |
| A | HIS154 |
| A | HIS192 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE EDO A 403 |
| Chain | Residue |
| A | ARG108 |
| A | GLY148 |
| A | LYS187 |
| A | PHE320 |
| A | TYR321 |
| A | HOH701 |
| A | HOH788 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CA A 404 |
| Chain | Residue |
| A | ARG225 |
| A | ARG245 |
| B | ARG225 |
| B | ARG245 |
| site_id | AC5 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CA A 405 |
| Chain | Residue |
| A | ARG245 |
| B | HOH689 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE ZN B 401 |
| Chain | Residue |
| B | HIS31 |
| B | HIS33 |
| B | KCX117 |
| B | ASP268 |
| B | ZN402 |
| B | HOH636 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN B 402 |
| Chain | Residue |
| B | KCX117 |
| B | HIS154 |
| B | HIS192 |
| B | ZN401 |
| B | HOH636 |
| site_id | AC8 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE EDO B 403 |
| Chain | Residue |
| B | ARG108 |
| B | GLY148 |
| B | LYS187 |
| B | PHE320 |
| B | TYR321 |
| B | GLY322 |
| B | HOH754 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CA B 404 |
| Chain | Residue |
| A | ARG225 |
| A | ARG245 |
| B | ARG225 |
| B | ARG245 |
| site_id | BC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CA B 405 |
| Chain | Residue |
| A | HOH573 |
| B | ARG245 |
| B | THR247 |
| B | HOH687 |
