1JUE
1.8 A resolution structure of native lactococcus lactis dihydroorotate dehydrogenase A
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 | 6 |
| Details | BINDING SITE FOR RESIDUE MG A 850 |
| Chain | Residue |
| A | LYS33 |
| A | SER35 |
| A | HOH1023 |
| A | HOH1038 |
| A | HOH1115 |
| A | HOH1129 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG B 850 |
| Chain | Residue |
| B | HOH1968 |
| B | HOH2084 |
| B | LYS33 |
| B | SER35 |
| B | HOH1923 |
| site_id | AC3 |
| Number of Residues | 24 |
| Details | BINDING SITE FOR RESIDUE FMN A 800 |
| Chain | Residue |
| A | ALA18 |
| A | SER19 |
| A | GLY20 |
| A | LYS43 |
| A | SER44 |
| A | TYR58 |
| A | ASN67 |
| A | MET69 |
| A | ASN127 |
| A | LYS164 |
| A | VAL192 |
| A | ASN193 |
| A | GLY221 |
| A | ILE224 |
| A | THR248 |
| A | GLY249 |
| A | GLY250 |
| A | GLY271 |
| A | THR272 |
| A | ACY900 |
| A | HOH1006 |
| A | HOH1010 |
| A | HOH1015 |
| A | HOH1021 |
| site_id | AC4 |
| Number of Residues | 24 |
| Details | BINDING SITE FOR RESIDUE FMN B 1800 |
| Chain | Residue |
| B | ALA18 |
| B | SER19 |
| B | GLY20 |
| B | LYS43 |
| B | SER44 |
| B | TYR58 |
| B | ASN67 |
| B | MET69 |
| B | ASN127 |
| B | LYS164 |
| B | VAL192 |
| B | ASN193 |
| B | GLY221 |
| B | ILE224 |
| B | THR248 |
| B | GLY249 |
| B | GLY250 |
| B | GLY271 |
| B | THR272 |
| B | ACY1900 |
| B | HOH1902 |
| B | HOH1905 |
| B | HOH1906 |
| B | HOH1926 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE ACY A 900 |
| Chain | Residue |
| A | LYS43 |
| A | MET69 |
| A | GLY70 |
| A | LEU71 |
| A | CYS130 |
| A | ASN132 |
| A | FMN800 |
| site_id | AC6 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE ACY B 1900 |
| Chain | Residue |
| B | LYS43 |
| B | MET69 |
| B | GLY70 |
| B | LEU71 |
| B | CYS130 |
| B | ASN132 |
| B | FMN1800 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL B 1001 |
| Chain | Residue |
| A | LYS213 |
| A | PHE216 |
| B | LEU171 |
| B | ALA234 |
| B | ARG238 |
| B | HOH1972 |
| site_id | AC8 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL B 1002 |
| Chain | Residue |
| A | LEU171 |
| A | ALA234 |
| A | ARG238 |
| B | LYS213 |
| B | ASP214 |
| B | PHE216 |
| B | HOH1974 |
| site_id | AC9 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL A 1003 |
| Chain | Residue |
| A | TYR168 |
| A | PHE169 |
| A | HIS173 |
| A | HOH1161 |
| A | HOH1251 |
| B | HIS173 |
| site_id | BC1 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE GOL A 1004 |
| Chain | Residue |
| A | ALA9 |
| A | LYS10 |
| A | GLY94 |
| site_id | BC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE GOL B 1005 |
| Chain | Residue |
| B | ALA9 |
| B | LYS10 |
| B | GLU93 |
| B | GLY94 |
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Nucleophile"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 14 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"9032071","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9655329","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 14 |
| Details | Binding site: {} |
| Chain | Residue | Details |
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 |
| site_id | MCSA1 |
| Number of Residues | 2 |
| Details | M-CSA 892 |
| Chain | Residue | Details |
| A | LYS43 | electrostatic stabiliser |
| A | CYS130 | proton shuttle (general acid/base) |
| site_id | MCSA2 |
| Number of Residues | 2 |
| Details | M-CSA 892 |
| Chain | Residue | Details |
| B | LYS43 | electrostatic stabiliser |
| B | CYS130 | proton shuttle (general acid/base) |
