4BJH
Crystal Structure of the Aquifex Reactor Complex Formed by Dihydroorotase (H180A, H232A) with Dihydroorotate and Aspartate Transcarbamoylase with N-(phosphonacetyl)-L-aspartate (PALA)
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 | 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 | 5 |
| Details | BINDING SITE FOR RESIDUE ZN A 423 |
| Chain | Residue |
| A | HIS61 |
| A | HIS63 |
| A | ASP153 |
| A | ASP305 |
| A | HOH2018 |
| site_id | AC2 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE DOR A 425 |
| Chain | Residue |
| A | GLY154 |
| A | VAL277 |
| A | ASN278 |
| A | HIS309 |
| A | PRO322 |
| A | GLY323 |
| A | HOH2018 |
| A | HOH2081 |
| A | HOH2174 |
| A | HOH2216 |
| A | HIS63 |
| A | ARG65 |
| A | ASN95 |
| A | ASP153 |
| site_id | AC3 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE PAL B 292 |
| Chain | Residue |
| B | SER45 |
| B | THR46 |
| B | ARG47 |
| B | THR48 |
| B | SER72 |
| B | LYS75 |
| B | ARG97 |
| B | HIS126 |
| B | ARG159 |
| B | VAL160 |
| B | ARG213 |
| B | GLN215 |
| B | GLY251 |
| B | HOH2059 |
| B | HOH2139 |
| B | HOH2140 |
| B | HOH2166 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE PO4 B 293 |
| Chain | Residue |
| B | PHE196 |
| B | ASP197 |
| B | ASP198 |
| B | LYS201 |
| B | EDO305 |
| B | EDO309 |
| site_id | AC5 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE BA B 295 |
| Chain | Residue |
| B | GLU70 |
| B | GLU70 |
| B | GLU70 |
| B | BA296 |
| B | BA296 |
| B | HOH2075 |
| B | HOH2075 |
| B | HOH2080 |
| site_id | AC6 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE BA B 296 |
| Chain | Residue |
| B | GLU70 |
| B | GLU70 |
| B | GLU70 |
| B | BA295 |
| B | BA295 |
| B | EDO303 |
| B | EDO303 |
| B | EDO303 |
| site_id | AC7 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE BA B 297 |
| Chain | Residue |
| B | ASP9 |
| B | GLU14 |
| B | EDO306 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO B 301 |
| Chain | Residue |
| A | ASP101 |
| A | ASN102 |
| A | THR103 |
| A | ASP138 |
| B | HOH2182 |
| site_id | AC9 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE EDO B 302 |
| Chain | Residue |
| B | ARG47 |
| B | GLU77 |
| B | ASP81 |
| B | PRO252 |
| B | VAL253 |
| B | TYR265 |
| B | ILE271 |
| B | HOH2097 |
| site_id | BC1 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE EDO B 303 |
| Chain | Residue |
| B | ARG49 |
| B | LEU65 |
| B | LEU65 |
| B | VAL66 |
| B | SER67 |
| B | GLU70 |
| B | GLU70 |
| B | BA296 |
| B | BA296 |
| B | BA296 |
| site_id | BC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO B 304 |
| Chain | Residue |
| B | GLU43 |
| B | PRO99 |
| B | GLU217 |
| B | ARG218 |
| B | HOH2177 |
| site_id | BC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO B 305 |
| Chain | Residue |
| B | VAL195 |
| B | PO4293 |
| B | HOH2128 |
| site_id | BC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO B 306 |
| Chain | Residue |
| B | SER3 |
| B | ASP9 |
| B | PHE288 |
| B | BA297 |
| site_id | BC5 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE EDO B 307 |
| Chain | Residue |
| A | ASP101 |
| A | ASN102 |
| site_id | BC6 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO B 308 |
| Chain | Residue |
| B | GLU13 |
| B | GLU16 |
| B | ARG12 |
| site_id | BC7 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO B 309 |
| Chain | Residue |
| B | VAL195 |
| B | ASP197 |
| B | PO4293 |
| site_id | BC8 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO B 310 |
| Chain | Residue |
| A | GLN222 |
| A | GLU240 |
| A | HOH2138 |
| site_id | BC9 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE EDO B 311 |
| Chain | Residue |
| A | TYR140 |
| B | ASP198 |
| B | VAL199 |
| B | ASP200 |
| B | GLN233 |
| B | ARG240 |
| B | HOH2154 |
| site_id | CC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE EDO B 312 |
| Chain | Residue |
| A | LEU200 |
| A | HOH2119 |
| B | SER6 |
| B | LEU8 |
| B | TYR105 |
| B | HIS124 |
| B | HOH2011 |
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 | 1 |
| Details | Active site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00220","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 3 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"15826652","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19128030","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"24314009","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1XRF","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1XRT","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3D6N","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4BJH","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00220","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"24314009","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"4BJH","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"19128030","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"24314009","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3D6N","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4BJH","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 10 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00001","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
