1XRT
The Crystal Structure of a Novel, Latent Dihydroorotase from Aquifex Aeolicus at 1.7 A Resolution
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 1423 |
| Chain | Residue |
| A | HIS61 |
| A | HIS63 |
| A | ASP153 |
| A | CYS181 |
| A | ASP305 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN B 1424 |
| Chain | Residue |
| B | ASP305 |
| B | HIS61 |
| B | HIS63 |
| B | ASP153 |
| B | CYS181 |
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 | ASP305 | |
| B | ASP305 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:15826652, ECO:0000269|PubMed:19128030, ECO:0000269|PubMed:24314009, ECO:0007744|PDB:1XRF, ECO:0007744|PDB:1XRT, ECO:0007744|PDB:3D6N, ECO:0007744|PDB:4BJH |
| Chain | Residue | Details |
| A | HIS61 | |
| A | HIS63 | |
| A | ASP153 | |
| B | HIS61 | |
| B | HIS63 | |
| B | ASP153 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00220, ECO:0000305|PubMed:24314009, ECO:0007744|PDB:4BJH |
| Chain | Residue | Details |
| A | ASN95 | |
| A | ASN278 | |
| A | HIS309 | |
| A | PRO322 | |
| B | ASN95 | |
| B | ASN278 | |
| B | HIS309 | |
| B | PRO322 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:19128030, ECO:0000269|PubMed:24314009, ECO:0007744|PDB:3D6N, ECO:0007744|PDB:4BJH |
| Chain | Residue | Details |
| A | ASP305 | |
| B | ASP305 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1j79 |
| Chain | Residue | Details |
| A | ASP305 |
| site_id | CSA2 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1j79 |
| Chain | Residue | Details |
| B | ASP305 |
