1KM0
Crystal structure of orotidine monophosphate decarboxylase mutant D70N 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 | 19 |
| Details | BINDING SITE FOR RESIDUE UP6 A 5001 |
| Chain | Residue |
| A | ASP20 |
| A | ARG203 |
| A | HOH4002 |
| A | HOH4007 |
| A | HOH4019 |
| A | HOH4020 |
| A | HOH4033 |
| A | HOH4115 |
| B | ASP75 |
| B | ILE76 |
| B | THR79 |
| A | LYS42 |
| A | ASN70 |
| A | LYS72 |
| A | MET126 |
| A | SER127 |
| A | PRO180 |
| A | GLN185 |
| A | GLY202 |
| site_id | AC2 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE UP6 B 5002 |
| Chain | Residue |
| A | ASP75 |
| A | ILE76 |
| A | THR79 |
| B | ASP20 |
| B | LYS42 |
| B | ASN70 |
| B | LYS72 |
| B | MET126 |
| B | SER127 |
| B | PRO180 |
| B | GLN185 |
| B | GLY202 |
| B | ARG203 |
| B | HOH4009 |
| B | HOH4016 |
| B | HOH4021 |
| B | HOH4034 |
| B | HOH4047 |
| B | HOH4095 |
| site_id | AC3 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE UP6 C 5003 |
| Chain | Residue |
| C | ASP20 |
| C | LYS42 |
| C | ASN70 |
| C | LYS72 |
| C | MET126 |
| C | SER127 |
| C | PRO180 |
| C | GLN185 |
| C | GLY202 |
| C | ARG203 |
| C | HOH4004 |
| C | HOH4010 |
| C | HOH4029 |
| C | HOH4051 |
| C | HOH4057 |
| C | HOH4061 |
| D | ASP75 |
| D | ILE76 |
| D | THR79 |
| site_id | AC4 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE UP6 D 5004 |
| Chain | Residue |
| C | ASP75 |
| C | ILE76 |
| C | THR79 |
| D | ASP20 |
| D | LYS42 |
| D | ASN70 |
| D | LYS72 |
| D | MET126 |
| D | SER127 |
| D | PRO180 |
| D | GLN185 |
| D | VAL201 |
| D | GLY202 |
| D | ARG203 |
| D | HOH4003 |
| D | HOH4012 |
| D | HOH4031 |
| D | HOH4038 |
| D | HOH4039 |
| D | HOH4105 |
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 | LYS72 | |
| C | LYS72 | |
| D | LYS72 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 28 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | ASP20 | |
| B | ASN70 | |
| B | SER127 | |
| B | PRO180 | |
| B | GLY202 | |
| B | ARG203 | |
| C | ASP20 | |
| C | LYS42 | |
| C | ASN70 | |
| C | SER127 | |
| C | PRO180 | |
| A | LYS42 | |
| C | GLY202 | |
| C | ARG203 | |
| D | ASP20 | |
| D | LYS42 | |
| D | ASN70 | |
| D | SER127 | |
| D | PRO180 | |
| D | GLY202 | |
| D | ARG203 | |
| A | ASN70 | |
| A | SER127 | |
| A | PRO180 | |
| A | GLY202 | |
| A | ARG203 | |
| B | ASP20 | |
| B | LYS42 |
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 | ASN70 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1dbt |
| Chain | Residue | Details |
| B | LYS72 | |
| B | ASN70 |
| site_id | CSA3 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1dbt |
| Chain | Residue | Details |
| C | LYS72 | |
| C | ASN70 |
| site_id | CSA4 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1dbt |
| Chain | Residue | Details |
| D | LYS72 | |
| D | ASN70 |
| 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 | ASN70 |
| site_id | CSA6 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1dbt |
| Chain | Residue | Details |
| B | LYS42 | |
| B | ASP75 | |
| B | LYS72 | |
| B | ASN70 |
| site_id | CSA7 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1dbt |
| Chain | Residue | Details |
| C | LYS42 | |
| C | ASP75 | |
| C | LYS72 | |
| C | ASN70 |
| site_id | CSA8 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1dbt |
| Chain | Residue | Details |
| D | LYS42 | |
| D | ASP75 | |
| D | LYS72 | |
| D | ASN70 |
