1EP1
CRYSTAL STRUCTURE OF LACTOCOCCUS LACTIS DIHYDROOROTATE DEHYDROGENASE B
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004152 | molecular_function | dihydroorotate dehydrogenase activity |
| A | 0004589 | molecular_function | dihydroorotate dehydrogenase (NAD+) activity |
| A | 0005515 | molecular_function | protein binding |
| 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 |
| B | 0005515 | molecular_function | protein binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0006221 | biological_process | pyrimidine nucleotide biosynthetic process |
| B | 0009055 | molecular_function | electron transfer activity |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0044205 | biological_process | 'de novo' UMP biosynthetic process |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| B | 0051536 | molecular_function | iron-sulfur cluster binding |
| B | 0051537 | molecular_function | 2 iron, 2 sulfur cluster binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE FMN A 501 |
| Chain | Residue |
| A | ALA23 |
| A | ILE196 |
| A | ASN197 |
| A | THR198 |
| A | SER221 |
| A | GLY222 |
| A | MET247 |
| A | GLY248 |
| A | GLY249 |
| A | GLY270 |
| A | THR271 |
| A | SER24 |
| A | HOH1001 |
| A | HOH1010 |
| A | HOH1088 |
| A | GLY25 |
| A | CYS26 |
| A | ALA49 |
| A | ASN72 |
| A | ASN104 |
| A | ASN132 |
| A | LYS170 |
| site_id | AC2 |
| Number of Residues | 23 |
| Details | BINDING SITE FOR RESIDUE FAD B 502 |
| Chain | Residue |
| A | GLU65 |
| B | LEU51 |
| B | ARG53 |
| B | PRO54 |
| B | ILE55 |
| B | SER56 |
| B | LEU70 |
| B | TYR71 |
| B | ARG72 |
| B | THR78 |
| B | GLY79 |
| B | THR80 |
| B | ILE120 |
| B | GLU221 |
| B | SER222 |
| B | ARG223 |
| B | MET224 |
| B | HOH1051 |
| B | HOH1054 |
| B | HOH1063 |
| B | HOH1073 |
| B | HOH1078 |
| B | HOH1190 |
| site_id | AC3 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE FES B 503 |
| Chain | Residue |
| B | MET224 |
| B | ALA225 |
| B | CYS226 |
| B | GLY227 |
| B | GLY229 |
| B | CYS231 |
| B | TYR232 |
| B | CYS234 |
| B | CYS249 |
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 7 |
| Details | BINDING: |
| Chain | Residue | Details |
| B | ARG53 | |
| B | LEU70 | |
| B | GLY79 | |
| B | CYS226 | |
| B | CYS231 | |
| B | CYS234 | |
| B | CYS249 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 11 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | SER24 | |
| A | GLY248 | |
| A | GLY270 | |
| A | LYS48 | |
| A | ASN72 | |
| A | ASN104 | |
| A | ASN132 | |
| A | LYS170 | |
| A | ILE196 | |
| A | ASN197 | |
| A | GLY222 |
