3D6N
Crystal Structure of Aquifex Dihydroorotase Activated by Aspartate Transcarbamoylase
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 | 0004070 | molecular_function | aspartate carbamoyltransferase activity |
| B | 0005829 | cellular_component | cytosol |
| B | 0006207 | biological_process | 'de novo' pyrimidine nucleobase biosynthetic process |
| B | 0006221 | biological_process | pyrimidine nucleotide biosynthetic process |
| B | 0006520 | biological_process | amino acid metabolic process |
| B | 0016597 | molecular_function | amino acid binding |
| B | 0016740 | molecular_function | transferase activity |
| B | 0016743 | molecular_function | carboxyl- or carbamoyltransferase activity |
| B | 0044205 | biological_process | 'de novo' UMP biosynthetic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 423 |
| Chain | Residue |
| A | HIS61 |
| A | HIS63 |
| A | ASP153 |
| A | ASP305 |
| site_id | AC2 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE FLC A 424 |
| Chain | Residue |
| A | HIS180 |
| A | HIS232 |
| A | ASN278 |
| A | ASP305 |
| A | ALA307 |
| A | HIS309 |
| A | PRO322 |
| A | GLY323 |
| A | HIS63 |
| A | ARG65 |
| A | ASN95 |
| A | ASP153 |
| A | GLY154 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE FLC B 292 |
| Chain | Residue |
| B | THR48 |
| B | ARG97 |
| B | HIS126 |
| B | ARG159 |
| B | ARG213 |
| B | GLY251 |
Functional Information from PROSITE/UniProt
| site_id | PS00097 |
| Number of Residues | 8 |
| Details | CARBAMOYLTRANSFERASE Aspartate and ornithine carbamoyltransferases signature. FsEpSTRT |
| Chain | Residue | Details |
| B | PHE41-THR48 |
| site_id | PS00482 |
| Number of Residues | 9 |
| Details | DIHYDROOROTASE_1 Dihydroorotase signature 1. DIHVHLRdP |
| Chain | Residue | Details |
| A | ASP59-PRO67 |
| site_id | PS00483 |
| Number of Residues | 12 |
| Details | DIHYDROOROTASE_2 Dihydroorotase signature 2. ATDhAPHqtfeK |
| Chain | Residue | Details |
| A | ALA303-LYS314 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 10 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00001 |
| Chain | Residue | Details |
| B | ARG47 | |
| B | PRO252 | |
| B | THR48 | |
| B | LYS75 | |
| B | ARG97 | |
| B | HIS126 | |
| B | GLN129 | |
| B | ARG159 | |
| B | ARG213 | |
| B | GLY251 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 3 |
| 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 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| 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 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:19128030, ECO:0000269|PubMed:24314009, ECO:0007744|PDB:3D6N, ECO:0007744|PDB:4BJH |
| Chain | Residue | Details |
| A | ASP305 |
