1JQX
The R57A mutant of 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 314 |
| Chain | Residue |
| A | LYS33 |
| A | SER35 |
| A | HOH1331 |
| A | HOH1365 |
| A | HOH1421 |
| A | HOH1489 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG B 314 |
| Chain | Residue |
| B | HOH2364 |
| B | HOH2421 |
| B | HOH2554 |
| B | LYS33 |
| B | SER35 |
| B | HOH2344 |
| site_id | AC3 |
| Number of Residues | 24 |
| Details | BINDING SITE FOR RESIDUE FMN A 1312 |
| 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 | ORO1313 |
| A | HOH1314 |
| A | HOH1316 |
| A | HOH1319 |
| A | HOH1399 |
| site_id | AC4 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE ORO A 1313 |
| Chain | Residue |
| A | LYS43 |
| A | ASN67 |
| A | MET69 |
| A | GLY70 |
| A | LEU71 |
| A | ASN127 |
| A | CYS130 |
| A | PRO131 |
| A | ASN132 |
| A | ASN193 |
| A | SER194 |
| A | FMN1312 |
| site_id | AC5 |
| Number of Residues | 24 |
| Details | BINDING SITE FOR RESIDUE FMN B 2312 |
| Chain | Residue |
| B | ALA18 |
| B | SER19 |
| B | GLY20 |
| B | LYS43 |
| B | SER44 |
| B | ASN67 |
| B | MET69 |
| B | ASN127 |
| B | LYS164 |
| B | VAL192 |
| B | ASN193 |
| B | SER194 |
| B | GLY221 |
| B | ILE224 |
| B | THR248 |
| B | GLY249 |
| B | GLY250 |
| B | GLY271 |
| B | THR272 |
| B | ORO2313 |
| B | HOH2314 |
| B | HOH2325 |
| B | HOH2333 |
| B | HOH2471 |
| site_id | AC6 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE ORO B 2313 |
| Chain | Residue |
| B | LYS43 |
| B | ASN67 |
| B | MET69 |
| B | GLY70 |
| B | LEU71 |
| B | ASN127 |
| B | CYS130 |
| B | PRO131 |
| B | ASN132 |
| B | ASN193 |
| B | SER194 |
| B | FMN2312 |
| site_id | AC7 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL B 1001 |
| Chain | Residue |
| A | LYS213 |
| A | PHE216 |
| A | HOH1636 |
| B | LEU171 |
| B | ALA234 |
| B | ARG238 |
| B | HOH2384 |
| B | HOH2610 |
| 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 | PHE216 |
| B | HOH2399 |
| B | HOH2604 |
| site_id | AC9 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL A 1003 |
| Chain | Residue |
| A | TYR168 |
| A | PHE169 |
| A | ASP170 |
| A | HIS173 |
| A | HOH1353 |
| A | HOH1371 |
| A | HOH1594 |
| B | HIS173 |
Functional Information from PROSITE/UniProt
| site_id | PS00912 |
| Number of Residues | 21 |
| Details | DHODEHASE_2 Dihydroorotate dehydrogenase signature 2. IIGtGGIeTgqdAfeHLlCGA |
| Chain | Residue | Details |
| A | ILE245-ALA265 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: Nucleophile |
| Chain | Residue | Details |
| A | CYS130 | |
| B | CYS130 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 12 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:9032071, ECO:0000269|PubMed:9655329 |
| Chain | Residue | Details |
| A | SER19 | |
| B | GLY221 | |
| B | GLY249 | |
| B | GLY271 | |
| A | LYS164 | |
| A | VAL192 | |
| A | GLY221 | |
| A | GLY249 | |
| A | GLY271 | |
| B | SER19 | |
| B | LYS164 | |
| B | VAL192 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 8 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | LYS43 | |
| A | ASN67 | |
| A | ASN127 | |
| A | ASN193 | |
| B | LYS43 | |
| B | ASN67 | |
| B | ASN127 | |
| B | ASN193 |
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) |
