1LOS
crystal structure of orotidine monophosphate decarboxylase mutant deltaR203A complexed with 6-azaUMP
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004590 | molecular_function | orotidine-5'-phosphate decarboxylase activity |
A | 0005829 | cellular_component | cytosol |
A | 0006207 | biological_process | 'de novo' pyrimidine nucleobase biosynthetic process |
A | 0006221 | biological_process | pyrimidine nucleotide biosynthetic process |
A | 0016831 | molecular_function | carboxy-lyase activity |
A | 0044205 | biological_process | 'de novo' UMP biosynthetic process |
B | 0004590 | molecular_function | orotidine-5'-phosphate decarboxylase activity |
B | 0005829 | cellular_component | cytosol |
B | 0006207 | biological_process | 'de novo' pyrimidine nucleobase biosynthetic process |
B | 0006221 | biological_process | pyrimidine nucleotide biosynthetic process |
B | 0016831 | molecular_function | carboxy-lyase activity |
B | 0044205 | biological_process | 'de novo' UMP biosynthetic process |
C | 0004590 | molecular_function | orotidine-5'-phosphate decarboxylase activity |
C | 0005829 | cellular_component | cytosol |
C | 0006207 | biological_process | 'de novo' pyrimidine nucleobase biosynthetic process |
C | 0006221 | biological_process | pyrimidine nucleotide biosynthetic process |
C | 0016831 | molecular_function | carboxy-lyase activity |
C | 0044205 | biological_process | 'de novo' UMP biosynthetic process |
D | 0004590 | molecular_function | orotidine-5'-phosphate decarboxylase activity |
D | 0005829 | cellular_component | cytosol |
D | 0006207 | biological_process | 'de novo' pyrimidine nucleobase biosynthetic process |
D | 0006221 | biological_process | pyrimidine nucleotide biosynthetic process |
D | 0016831 | molecular_function | carboxy-lyase activity |
D | 0044205 | biological_process | 'de novo' UMP biosynthetic process |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 20 |
Details | BINDING SITE FOR RESIDUE UP6 A 5001 |
Chain | Residue |
A | ALA18 |
A | HOH4016 |
A | HOH4024 |
A | HOH4033 |
A | HOH4036 |
A | HOH4037 |
A | HOH4087 |
A | HOH4088 |
A | HOH4206 |
B | ASP1075 |
B | ILE1076 |
A | ASP20 |
B | THR1079 |
A | LYS42 |
A | LYS72 |
A | MET126 |
A | SER127 |
A | PRO180 |
A | GLY202 |
A | ALA203 |
site_id | AC2 |
Number of Residues | 17 |
Details | BINDING SITE FOR RESIDUE UP6 B 5002 |
Chain | Residue |
A | ASP75 |
A | ILE76 |
A | THR79 |
B | ALA1018 |
B | ASP1020 |
B | LYS1042 |
B | LYS1072 |
B | MET1126 |
B | SER1127 |
B | PRO1180 |
B | GLY1202 |
B | ALA1203 |
B | HOH4057 |
B | HOH4061 |
B | HOH4069 |
B | HOH4148 |
B | HOH4152 |
site_id | AC3 |
Number of Residues | 15 |
Details | BINDING SITE FOR RESIDUE UP6 C 5003 |
Chain | Residue |
C | ALA2018 |
C | ASP2020 |
C | LYS2042 |
C | LYS2072 |
C | MET2126 |
C | SER2127 |
C | PRO2180 |
C | GLY2202 |
C | ALA2203 |
C | HOH4154 |
C | HOH4156 |
C | HOH4169 |
D | ASP3075 |
D | ILE3076 |
D | THR3079 |
site_id | AC4 |
Number of Residues | 16 |
Details | BINDING SITE FOR RESIDUE UP6 D 5004 |
Chain | Residue |
C | ASP2075 |
C | ILE2076 |
C | THR2079 |
D | ASP3020 |
D | LYS3042 |
D | LYS3072 |
D | MET3126 |
D | SER3127 |
D | PRO3180 |
D | GLY3202 |
D | ALA3203 |
D | HOH4054 |
D | HOH4161 |
D | HOH4193 |
D | HOH4195 |
D | HOH4205 |
Functional Information from PROSITE/UniProt
site_id | PS00156 |
Number of Residues | 14 |
Details | OMPDECASE Orotidine 5'-phosphate decarboxylase active site. IIaDfKvaDIPeTN |
Chain | Residue | Details |
A | ILE67-ASN80 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 4 |
Details | ACT_SITE: Proton donor |
Chain | Residue | Details |
A | LYS72 | |
B | LYS1072 | |
C | LYS2072 | |
D | LYS3072 |
site_id | SWS_FT_FI2 |
Number of Residues | 28 |
Details | BINDING: |
Chain | Residue | Details |
A | ASP20 | |
B | ASP1070 | |
B | SER1127 | |
B | PRO1180 | |
B | TYR1206 | |
B | LEU1207 | |
C | ASP2020 | |
C | LYS2042 | |
C | ASP2070 | |
C | SER2127 | |
C | PRO2180 | |
A | LYS42 | |
C | TYR2206 | |
C | LEU2207 | |
D | ASP3020 | |
D | LYS3042 | |
D | ASP3070 | |
D | SER3127 | |
D | PRO3180 | |
D | TYR3206 | |
D | LEU3207 | |
A | ASP70 | |
A | SER127 | |
A | PRO180 | |
A | TYR206 | |
A | LEU207 | |
B | ASP1020 | |
B | LYS1042 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1dbt |
Chain | Residue | Details |
A | LYS72 | |
A | ASP70 |
site_id | CSA2 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1dbt |
Chain | Residue | Details |
B | ASP1070 | |
B | LYS1072 |
site_id | CSA3 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1dbt |
Chain | Residue | Details |
C | LYS2072 | |
C | ASP2070 |
site_id | CSA4 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1dbt |
Chain | Residue | Details |
D | ASP3070 | |
D | LYS3072 |
site_id | CSA5 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1dbt |
Chain | Residue | Details |
A | LYS42 | |
A | ASP75 | |
A | LYS72 | |
A | ASP70 |
site_id | CSA6 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1dbt |
Chain | Residue | Details |
B | ASP1070 | |
B | ASP1075 | |
B | LYS1072 | |
B | LYS1042 |
site_id | CSA7 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1dbt |
Chain | Residue | Details |
C | LYS2042 | |
C | LYS2072 | |
C | ASP2075 | |
C | ASP2070 |
site_id | CSA8 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1dbt |
Chain | Residue | Details |
D | LYS3042 | |
D | LYS3072 | |
D | ASP3070 | |
D | ASP3075 |