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 | ACT_SITE: ACT_SITE => ECO:0000255|HAMAP-Rule:MF_00220 |
Chain | Residue | Details |
A | ASP303 | |
B | ASP303 |
site_id | SWS_FT_FI2 |
Number of Residues | 20 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00220 |
Chain | Residue | Details |
A | HIS58 | |
A | PHE321 | |
B | HIS58 | |
B | HIS60 | |
B | ASN92 | |
B | ASP150 | |
B | HIS177 | |
B | HIS230 | |
B | ASN276 | |
B | ASP303 | |
B | HIS307 | |
A | HIS60 | |
B | PHE321 | |
A | ASN92 | |
A | ASP150 | |
A | HIS177 | |
A | HIS230 | |
A | ASN276 | |
A | ASP303 | |
A | HIS307 |