3C3N
Crystal structure of dihydroorotate dehydrogenase from Trypanosoma cruzi strain Y
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004152 | molecular_function | dihydroorotate dehydrogenase activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0006207 | biological_process | 'de novo' pyrimidine nucleobase biosynthetic process |
| A | 0006221 | biological_process | pyrimidine nucleotide biosynthetic process |
| A | 0006222 | biological_process | UMP biosynthetic process |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0016627 | molecular_function | oxidoreductase activity, acting on the CH-CH group of donors |
| A | 0044205 | biological_process | 'de novo' UMP biosynthetic process |
| A | 1990663 | molecular_function | dihydroorotate dehydrogenase (fumarate) activity |
| B | 0004152 | molecular_function | dihydroorotate dehydrogenase activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0006207 | biological_process | 'de novo' pyrimidine nucleobase biosynthetic process |
| B | 0006221 | biological_process | pyrimidine nucleotide biosynthetic process |
| B | 0006222 | biological_process | UMP biosynthetic process |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0016627 | molecular_function | oxidoreductase activity, acting on the CH-CH group of donors |
| B | 0044205 | biological_process | 'de novo' UMP biosynthetic process |
| B | 1990663 | molecular_function | dihydroorotate dehydrogenase (fumarate) activity |
| C | 0004152 | molecular_function | dihydroorotate dehydrogenase activity |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0006207 | biological_process | 'de novo' pyrimidine nucleobase biosynthetic process |
| C | 0006221 | biological_process | pyrimidine nucleotide biosynthetic process |
| C | 0006222 | biological_process | UMP biosynthetic process |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0016627 | molecular_function | oxidoreductase activity, acting on the CH-CH group of donors |
| C | 0044205 | biological_process | 'de novo' UMP biosynthetic process |
| C | 1990663 | molecular_function | dihydroorotate dehydrogenase (fumarate) activity |
| D | 0004152 | molecular_function | dihydroorotate dehydrogenase activity |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0006207 | biological_process | 'de novo' pyrimidine nucleobase biosynthetic process |
| D | 0006221 | biological_process | pyrimidine nucleotide biosynthetic process |
| D | 0006222 | biological_process | UMP biosynthetic process |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0016627 | molecular_function | oxidoreductase activity, acting on the CH-CH group of donors |
| D | 0044205 | biological_process | 'de novo' UMP biosynthetic process |
| D | 1990663 | molecular_function | dihydroorotate dehydrogenase (fumarate) activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE SO4 A 600 |
| Chain | Residue |
| A | LYS45 |
| A | HOH335 |
| A | HOH406 |
| A | ASN69 |
| A | MET71 |
| A | GLY72 |
| A | LEU73 |
| A | PRO74 |
| A | CYS132 |
| A | ASN134 |
| A | FMN315 |
| site_id | AC2 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE SO4 B 600 |
| Chain | Residue |
| B | LYS45 |
| B | ASN69 |
| B | MET71 |
| B | GLY72 |
| B | LEU73 |
| B | PRO74 |
| B | CYS132 |
| B | ASN134 |
| B | FMN315 |
| B | HOH349 |
| B | HOH402 |
| site_id | AC3 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE SO4 C 600 |
| Chain | Residue |
| C | LYS45 |
| C | ASN69 |
| C | MET71 |
| C | GLY72 |
| C | LEU73 |
| C | PRO74 |
| C | CYS132 |
| C | ASN134 |
| C | FMN316 |
| C | HOH357 |
| C | HOH405 |
| site_id | AC4 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE SO4 D 600 |
| Chain | Residue |
| D | LYS45 |
| D | ASN69 |
| D | MET71 |
| D | GLY72 |
| D | LEU73 |
| D | PRO74 |
| D | CYS132 |
| D | ASN134 |
| D | FMN316 |
| D | HOH377 |
| D | HOH426 |
| site_id | AC5 |
| Number of Residues | 25 |
| Details | BINDING SITE FOR RESIDUE FMN A 315 |
| Chain | Residue |
| A | ALA20 |
| A | ALA21 |
| A | GLY22 |
| A | LYS45 |
| A | SER46 |
| A | TYR60 |
| A | ASN69 |
| A | MET71 |
| A | ASN129 |
| A | LYS166 |
| A | VAL195 |
| A | ASN196 |
| A | SER197 |
| A | GLY223 |
| A | GLY224 |
| A | ILE227 |
| A | CYS250 |
| A | GLY251 |
| A | GLY252 |
| A | GLY273 |
| A | THR274 |
| A | HOH387 |
| A | HOH394 |
| A | HOH510 |
| A | SO4600 |
| site_id | AC6 |
| Number of Residues | 24 |
| Details | BINDING SITE FOR RESIDUE FMN B 315 |
| Chain | Residue |
| B | ALA20 |
| B | ALA21 |
| B | GLY22 |
| B | LYS45 |
| B | SER46 |
| B | TYR60 |
| B | ASN69 |
| B | ASN129 |
| B | LYS166 |
| B | VAL195 |
| B | ASN196 |
| B | SER197 |
| B | GLY224 |
| B | ILE227 |
| B | CYS250 |
| B | GLY251 |
| B | GLY252 |
| B | GLY273 |
| B | THR274 |
| B | HOH389 |
| B | HOH431 |
| B | HOH498 |
| B | HOH507 |
| B | SO4600 |
| site_id | AC7 |
| Number of Residues | 26 |
| Details | BINDING SITE FOR RESIDUE FMN C 316 |
| Chain | Residue |
| C | ASN69 |
| C | MET71 |
| C | ASN129 |
| C | LYS166 |
| C | VAL195 |
| C | ASN196 |
| C | SER197 |
| C | GLY223 |
| C | GLY224 |
| C | ILE227 |
| C | CYS250 |
| C | GLY251 |
| C | GLY252 |
| C | GLY273 |
| C | THR274 |
| C | HOH394 |
| C | HOH428 |
| C | HOH460 |
| C | HOH484 |
| C | SO4600 |
| C | ALA20 |
| C | ALA21 |
| C | GLY22 |
| C | LYS45 |
| C | SER46 |
| C | TYR60 |
| site_id | AC8 |
| Number of Residues | 25 |
| Details | BINDING SITE FOR RESIDUE FMN D 316 |
| Chain | Residue |
| D | ALA20 |
| D | ALA21 |
| D | GLY22 |
| D | LYS45 |
| D | SER46 |
| D | ASN69 |
| D | MET71 |
| D | ASN129 |
| D | LYS166 |
| D | VAL195 |
| D | ASN196 |
| D | SER197 |
| D | GLY223 |
| D | GLY224 |
| D | ILE227 |
| D | CYS250 |
| D | GLY251 |
| D | GLY252 |
| D | GLY273 |
| D | THR274 |
| D | HOH358 |
| D | HOH414 |
| D | HOH447 |
| D | HOH475 |
| D | SO4600 |
| site_id | AC9 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL A 316 |
| Chain | Residue |
| A | LYS216 |
| A | GLN217 |
| A | PHE219 |
| A | HOH334 |
| A | HOH373 |
| D | ILE173 |
| D | ALA237 |
| D | ARG241 |
| site_id | BC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL A 317 |
| Chain | Residue |
| A | TYR170 |
| A | PHE171 |
| A | HIS175 |
| D | PHE171 |
| D | HIS175 |
| site_id | BC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL B 316 |
| Chain | Residue |
| B | TYR170 |
| B | PHE171 |
| B | HIS175 |
| B | HOH478 |
| C | PHE171 |
| C | HIS175 |
| site_id | BC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL C 2 |
| Chain | Residue |
| B | LYS216 |
| B | GLN217 |
| B | PHE219 |
| C | ILE173 |
| C | ARG241 |
| C | HOH456 |
| site_id | BC4 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE GOL D 317 |
| Chain | Residue |
| D | GLU257 |
| D | HOH351 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | ACT_SITE: Nucleophile => ECO:0000250 |
| Chain | Residue | Details |
| A | CYS132 | |
| B | CYS132 | |
| C | CYS132 | |
| D | CYS132 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 24 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:18302934 |
| Chain | Residue | Details |
| A | ALA21 | |
| B | GLY224 | |
| B | GLY251 | |
| B | GLY273 | |
| C | ALA21 | |
| C | LYS166 | |
| C | VAL195 | |
| C | GLY224 | |
| C | GLY251 | |
| C | GLY273 | |
| D | ALA21 | |
| A | LYS166 | |
| D | LYS166 | |
| D | VAL195 | |
| D | GLY224 | |
| D | GLY251 | |
| D | GLY273 | |
| A | VAL195 | |
| A | GLY224 | |
| A | GLY251 | |
| A | GLY273 | |
| B | ALA21 | |
| B | LYS166 | |
| B | VAL195 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 20 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | LYS45 | |
| B | ASN196 | |
| C | LYS45 | |
| C | ASN69 | |
| C | ASN129 | |
| C | ASN134 | |
| C | ASN196 | |
| D | LYS45 | |
| D | ASN69 | |
| D | ASN129 | |
| D | ASN134 | |
| A | ASN69 | |
| D | ASN196 | |
| A | ASN129 | |
| A | ASN134 | |
| A | ASN196 | |
| B | LYS45 | |
| B | ASN69 | |
| B | ASN129 | |
| B | ASN134 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 2dor |
| Chain | Residue | Details |
| A | LYS45 | |
| A | CYS132 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 2dor |
| Chain | Residue | Details |
| B | LYS45 | |
| B | CYS132 |
| site_id | CSA3 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 2dor |
| Chain | Residue | Details |
| C | LYS45 | |
| C | CYS132 |
| site_id | CSA4 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 2dor |
| Chain | Residue | Details |
| D | LYS45 | |
| D | CYS132 |
| site_id | CSA5 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 2dor |
| Chain | Residue | Details |
| A | CYS132 |
| site_id | CSA6 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 2dor |
| Chain | Residue | Details |
| B | CYS132 |
| site_id | CSA7 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 2dor |
| Chain | Residue | Details |
| C | CYS132 |
| site_id | CSA8 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 2dor |
| Chain | Residue | Details |
| D | CYS132 |
