1EP2
CRYSTAL STRUCTURE OF LACTOCOCCUS LACTIS DIHYDROOROTATE DEHYDROGENASE B COMPLEXED WITH OROTATE
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004152 | molecular_function | dihydroorotate dehydrogenase activity |
A | 0004589 | molecular_function | dihydroorotate dehydrogenase (NADH) 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 | ORO502 |
A | HOH1003 |
A | HOH1020 |
A | GLY25 |
A | LYS48 |
A | ALA49 |
A | ASN72 |
A | ASN104 |
A | ASN132 |
A | LYS170 |
site_id | AC2 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE ORO A 502 |
Chain | Residue |
A | LYS48 |
A | ASN72 |
A | ILE74 |
A | GLY75 |
A | LEU76 |
A | ASN132 |
A | CYS135 |
A | PRO136 |
A | ASN137 |
A | ASN197 |
A | THR198 |
A | FMN501 |
site_id | AC3 |
Number of Residues | 20 |
Details | BINDING SITE FOR RESIDUE FAD B 503 |
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 | HOH1006 |
B | HOH1046 |
B | HOH1050 |
site_id | AC4 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE FES B 504 |
Chain | Residue |
B | MET224 |
B | ALA225 |
B | CYS226 |
B | GLY227 |
B | GLY229 |
B | ALA230 |
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 |