1JUB
The K136E 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 850 |
Chain | Residue |
A | LYS33 |
A | SER35 |
A | HOH1103 |
A | HOH1141 |
A | HOH1162 |
A | HOH1262 |
site_id | AC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MG B 850 |
Chain | Residue |
B | HOH1996 |
B | HOH2054 |
B | LYS33 |
B | SER35 |
B | HOH1882 |
site_id | AC3 |
Number of Residues | 23 |
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 | HOH1005 |
A | HOH1011 |
A | HOH1012 |
A | HOH1017 |
site_id | AC4 |
Number of Residues | 23 |
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 | HOH1801 |
B | HOH1805 |
B | HOH1812 |
B | HOH1814 |
site_id | AC5 |
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 | HOH1876 |
site_id | AC6 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE GOL A 1002 |
Chain | Residue |
A | LEU171 |
A | ALA234 |
A | ARG238 |
A | HOH1104 |
B | LYS213 |
B | ASP214 |
B | PHE216 |
site_id | AC7 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE GOL A 1003 |
Chain | Residue |
A | TYR168 |
A | PHE169 |
A | HIS173 |
A | HOH1042 |
site_id | AC8 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE GOL A 1004 |
Chain | Residue |
A | ALA9 |
A | LYS10 |
A | GLY94 |
site_id | AC9 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE GOL B 1005 |
Chain | Residue |
B | ALA9 |
B | LYS10 |
B | GLY94 |
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
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) |