3GRI
The Crystal Structure of a Dihydroorotase from Staphylococcus aureus
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004038 | molecular_function | allantoinase activity |
| A | 0004151 | molecular_function | dihydroorotase activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0006145 | biological_process | purine nucleobase catabolic process |
| A | 0006221 | biological_process | pyrimidine nucleotide biosynthetic process |
| A | 0008270 | molecular_function | zinc ion binding |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0016810 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds |
| A | 0016812 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amides |
| A | 0044205 | biological_process | 'de novo' UMP biosynthetic process |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0004038 | molecular_function | allantoinase activity |
| B | 0004151 | molecular_function | dihydroorotase activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0006145 | biological_process | purine nucleobase catabolic process |
| B | 0006221 | biological_process | pyrimidine nucleotide biosynthetic process |
| B | 0008270 | molecular_function | zinc ion binding |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0016810 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds |
| B | 0016812 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amides |
| 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 | 5 |
| Details | BINDING SITE FOR RESIDUE ZN A 500 |
| Chain | Residue |
| A | HIS58 |
| A | HIS60 |
| A | ASP303 |
| A | HOH491 |
| A | HOH658 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CL A 600 |
| Chain | Residue |
| A | ILE124 |
| A | THR125 |
| A | HOH482 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CL A 601 |
| Chain | Residue |
| A | THR86 |
| A | TYR364 |
| A | ASP374 |
| A | HOH458 |
| A | THR85 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA A 700 |
| Chain | Residue |
| A | PHE391 |
| A | SER393 |
| A | HOH490 |
| A | HOH527 |
| A | HOH610 |
| A | HOH628 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CA A 701 |
| Chain | Residue |
| A | GLU104 |
| A | GLU142 |
| A | GLY199 |
| A | HOH433 |
| A | HOH517 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN B 500 |
| Chain | Residue |
| B | HIS58 |
| B | HIS60 |
| B | ASP303 |
| B | HOH492 |
| site_id | AC7 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CL B 600 |
| Chain | Residue |
| B | ILE124 |
| B | THR125 |
| B | HOH551 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CA B 700 |
| Chain | Residue |
| B | PHE391 |
| B | SER393 |
| B | HOH540 |
| B | HOH665 |
| site_id | AC9 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CA B 701 |
| Chain | Residue |
| B | GLU104 |
| B | GLU142 |
| B | GLY199 |
| B | HOH479 |
| B | HOH493 |
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00220","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 24 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00220","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1j79 |
| Chain | Residue | Details |
| A | ASP303 |
| site_id | CSA2 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1j79 |
| Chain | Residue | Details |
| B | ASP303 |
