1OVD
THE K136E MUTANT OF LACTOCOCCUS LACTIS DIHYDROOROTATE DEHYDROGENASE A IN COMPLEX WITH OROTATE
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 | HOH907 |
| A | HOH988 |
| A | HOH1074 |
| A | HOH1152 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG B 851 |
| Chain | Residue |
| B | HOH1066 |
| B | HOH1071 |
| B | LYS33 |
| B | SER35 |
| B | HOH985 |
| site_id | AC3 |
| Number of Residues | 22 |
| 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 | ASN127 |
| A | LYS164 |
| A | VAL192 |
| A | ASN193 |
| A | GLY221 |
| A | ILE224 |
| A | THR248 |
| A | GLY249 |
| A | GLY250 |
| A | GLY271 |
| A | THR272 |
| A | ORO900 |
| A | HOH912 |
| A | HOH993 |
| A | HOH995 |
| site_id | AC4 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE FMN B 801 |
| Chain | Residue |
| B | ALA18 |
| B | SER19 |
| B | GLY20 |
| B | LYS43 |
| B | SER44 |
| B | TYR58 |
| B | ASN67 |
| B | ASN127 |
| B | LYS164 |
| B | VAL192 |
| B | ASN193 |
| B | GLY221 |
| B | ILE224 |
| B | THR248 |
| B | GLY249 |
| B | GLY250 |
| B | GLY271 |
| B | THR272 |
| B | ORO901 |
| B | HOH902 |
| B | HOH904 |
| B | HOH990 |
| site_id | AC5 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE ORO A 900 |
| 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 | FMN800 |
| site_id | AC6 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE ORO B 901 |
| 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 | FMN801 |
| site_id | AC7 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL B 491 |
| Chain | Residue |
| A | LYS213 |
| A | ASP214 |
| A | PHE216 |
| B | LEU171 |
| B | ALA234 |
| B | ARG238 |
| B | HOH959 |
| site_id | AC8 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE GOL A 492 |
| Chain | Residue |
| A | ALA9 |
| A | LYS10 |
| A | GLY94 |
| site_id | AC9 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL A 493 |
| Chain | Residue |
| A | ALA234 |
| A | ARG238 |
| A | HOH1050 |
| B | LYS213 |
| B | ASP214 |
| B | PHE216 |
| site_id | BC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL B 494 |
| Chain | Residue |
| B | HOH1114 |
| B | ALA9 |
| B | LYS10 |
| B | GLU93 |
| B | GLY94 |
| site_id | BC2 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE GOL A 495 |
| Chain | Residue |
| A | TYR141 |
| A | TYR168 |
| A | PHE169 |
| A | ASP170 |
| A | HIS173 |
| A | HOH901 |
| A | HOH902 |
| B | TYR141 |
| B | TYR168 |
| B | PHE169 |
| B | HIS173 |
Functional Information from PROSITE/UniProt
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
