1DVJ
CRYSTAL STRUCTURE OF OROTIDINE MONOPHOSPHATE DECARBOXYLASE 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 | 16 |
Details | BINDING SITE FOR RESIDUE UP6 A 5001 |
Chain | Residue |
A | ASP20 |
A | HOH4001 |
A | HOH4016 |
A | HOH4065 |
A | HOH4068 |
A | HOH4076 |
A | HOH4125 |
A | HOH4140 |
A | LYS42 |
A | LYS72 |
A | MET126 |
A | SER127 |
A | PRO180 |
A | GLN185 |
A | GLY202 |
A | ARG203 |
site_id | AC2 |
Number of Residues | 15 |
Details | BINDING SITE FOR RESIDUE UP6 B 5002 |
Chain | Residue |
B | ASP20 |
B | LYS42 |
B | LYS72 |
B | MET126 |
B | SER127 |
B | PRO180 |
B | GLN185 |
B | GLY202 |
B | ARG203 |
B | HOH4024 |
B | HOH4025 |
B | HOH4028 |
B | HOH4036 |
B | HOH4081 |
B | HOH4142 |
site_id | AC3 |
Number of Residues | 16 |
Details | BINDING SITE FOR RESIDUE UP6 C 5003 |
Chain | Residue |
C | ASP20 |
C | LYS42 |
C | LYS72 |
C | MET126 |
C | SER127 |
C | PRO180 |
C | GLN185 |
C | GLY202 |
C | ARG203 |
C | HOH4003 |
C | HOH4012 |
C | HOH4021 |
C | HOH4023 |
C | HOH4066 |
C | HOH4101 |
C | HOH4139 |
site_id | AC4 |
Number of Residues | 15 |
Details | BINDING SITE FOR RESIDUE UP6 D 5004 |
Chain | Residue |
D | ASP20 |
D | LYS42 |
D | LYS72 |
D | MET126 |
D | SER127 |
D | PRO180 |
D | GLY202 |
D | ARG203 |
D | HOH4004 |
D | HOH4007 |
D | HOH4020 |
D | HOH4032 |
D | HOH4044 |
D | HOH4050 |
D | HOH4053 |
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 | LYS72 | |
C | LYS72 | |
D | LYS72 |
site_id | SWS_FT_FI2 |
Number of Residues | 28 |
Details | BINDING: |
Chain | Residue | Details |
A | ASP20 | |
B | ASP70 | |
B | SER127 | |
B | PRO180 | |
B | GLY202 | |
B | ARG203 | |
C | ASP20 | |
C | LYS42 | |
C | ASP70 | |
C | SER127 | |
C | PRO180 | |
A | LYS42 | |
C | GLY202 | |
C | ARG203 | |
D | ASP20 | |
D | LYS42 | |
D | ASP70 | |
D | SER127 | |
D | PRO180 | |
D | GLY202 | |
D | ARG203 | |
A | ASP70 | |
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 | ASP70 |
site_id | CSA2 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1dbt |
Chain | Residue | Details |
B | LYS72 | |
B | ASP70 |
site_id | CSA3 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1dbt |
Chain | Residue | Details |
C | LYS72 | |
C | ASP70 |
site_id | CSA4 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1dbt |
Chain | Residue | Details |
D | LYS72 | |
D | ASP70 |
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 | LYS42 | |
B | ASP75 | |
B | LYS72 | |
B | ASP70 |
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 | ASP70 |
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 | ASP70 |