2DJX
Crystal structure of native Trypanosoma cruzi dihydroorotate dehydrogenase
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 |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE NCO A 1351 |
Chain | Residue |
A | GLN275 |
A | GLU276 |
A | HOH1534 |
B | GLN275 |
B | GLU276 |
site_id | AC2 |
Number of Residues | 22 |
Details | BINDING SITE FOR RESIDUE FMN A 1350 |
Chain | Residue |
A | SER44 |
A | ASN67 |
A | ASN127 |
A | LYS164 |
A | VAL193 |
A | ASN194 |
A | SER195 |
A | GLY222 |
A | ILE225 |
A | CYS248 |
A | GLY249 |
A | GLY250 |
A | GLY271 |
A | THR272 |
A | HOH1474 |
A | HOH1488 |
A | HOH1494 |
A | HOH1543 |
A | ALA18 |
A | ALA19 |
A | GLY20 |
A | LYS43 |
site_id | AC3 |
Number of Residues | 21 |
Details | BINDING SITE FOR RESIDUE FMN B 2350 |
Chain | Residue |
B | ALA18 |
B | ALA19 |
B | GLY20 |
B | LYS43 |
B | SER44 |
B | ASN67 |
B | ASN127 |
B | LYS164 |
B | VAL193 |
B | ASN194 |
B | GLY222 |
B | ILE225 |
B | CYS248 |
B | GLY249 |
B | GLY250 |
B | GLY271 |
B | THR272 |
B | HOH2487 |
B | HOH2491 |
B | HOH2506 |
B | HOH2533 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | ACT_SITE: Nucleophile => ECO:0000250 |
Chain | Residue | Details |
A | CYS130 | |
B | CYS130 |
site_id | SWS_FT_FI2 |
Number of Residues | 12 |
Details | BINDING: BINDING => ECO:0000269|PubMed:18302934 |
Chain | Residue | Details |
A | ALA19 | |
B | GLY222 | |
B | GLY249 | |
B | GLY271 | |
A | LYS164 | |
A | VAL193 | |
A | GLY222 | |
A | GLY249 | |
A | GLY271 | |
B | ALA19 | |
B | LYS164 | |
B | VAL193 |
site_id | SWS_FT_FI3 |
Number of Residues | 10 |
Details | BINDING: |
Chain | Residue | Details |
A | LYS43 | |
B | ASN194 | |
A | ASN67 | |
A | ASN127 | |
A | ASN132 | |
A | ASN194 | |
B | LYS43 | |
B | ASN67 | |
B | ASN127 | |
B | ASN132 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 2dor |
Chain | Residue | Details |
A | LYS43 | |
A | CYS130 |
site_id | CSA2 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 2dor |
Chain | Residue | Details |
B | LYS43 | |
B | CYS130 |
site_id | CSA3 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 2dor |
Chain | Residue | Details |
A | CYS130 |
site_id | CSA4 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 2dor |
Chain | Residue | Details |
B | CYS130 |