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 | 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 |