1DQX
CRYSTAL STRUCTURE OF OROTIDINE 5'-PHOSPHATE DECARBOXYLASE COMPLEXED TO 6-HYDROXYURIDINE 5'-PHOSPHATE (BMP)
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 | 0006222 | biological_process | UMP biosynthetic process |
A | 0016829 | molecular_function | lyase activity |
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 | 0006222 | biological_process | UMP biosynthetic process |
B | 0016829 | molecular_function | lyase activity |
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 | 0006222 | biological_process | UMP biosynthetic process |
C | 0016829 | molecular_function | lyase activity |
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 | 0006222 | biological_process | UMP biosynthetic process |
D | 0016829 | molecular_function | lyase activity |
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 | 18 |
Details | BINDING SITE FOR RESIDUE BMP A 601 |
Chain | Residue |
A | SER35 |
A | GLN215 |
A | TYR217 |
A | GLY234 |
A | ARG235 |
A | HOH625 |
A | HOH628 |
B | ASP96 |
B | ILE97 |
B | THR100 |
A | ASP37 |
A | LYS59 |
A | HIS61 |
A | ASP91 |
A | LYS93 |
A | LEU153 |
A | SER154 |
A | PRO202 |
site_id | AC2 |
Number of Residues | 18 |
Details | BINDING SITE FOR RESIDUE BMP B 602 |
Chain | Residue |
A | ASP96 |
A | ILE97 |
A | THR100 |
B | SER35 |
B | ASP37 |
B | LYS59 |
B | HIS61 |
B | ASP91 |
B | LYS93 |
B | LEU153 |
B | SER154 |
B | PRO202 |
B | GLN215 |
B | TYR217 |
B | GLY234 |
B | ARG235 |
B | HOH630 |
B | HOH677 |
site_id | AC3 |
Number of Residues | 18 |
Details | BINDING SITE FOR RESIDUE BMP C 603 |
Chain | Residue |
C | SER35 |
C | ASP37 |
C | LYS59 |
C | HIS61 |
C | ASP91 |
C | LYS93 |
C | LEU153 |
C | SER154 |
C | PRO202 |
C | GLN215 |
C | TYR217 |
C | GLY234 |
C | ARG235 |
C | HOH622 |
C | HOH637 |
D | ASP96 |
D | ILE97 |
D | THR100 |
site_id | AC4 |
Number of Residues | 17 |
Details | BINDING SITE FOR RESIDUE BMP D 604 |
Chain | Residue |
C | ASP96 |
C | ILE97 |
C | THR100 |
D | SER35 |
D | ASP37 |
D | LYS59 |
D | HIS61 |
D | ASP91 |
D | LYS93 |
D | LEU153 |
D | SER154 |
D | PRO202 |
D | GLN215 |
D | TYR217 |
D | GLY234 |
D | ARG235 |
D | HOH609 |
Functional Information from PROSITE/UniProt
site_id | PS00156 |
Number of Residues | 14 |
Details | OMPDECASE Orotidine 5'-phosphate decarboxylase active site. LFeDrKfaDIGnTV |
Chain | Residue | Details |
A | LEU88-VAL101 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 4 |
Details | Active site: {"description":"Proton donor"} |
Chain | Residue | Details |
site_id | SWS_FT_FI2 |
Number of Residues | 56 |
Details | Binding site: {} |
Chain | Residue | Details |
site_id | SWS_FT_FI3 |
Number of Residues | 4 |
Details | Modified residue: {"description":"N-acetylserine","evidences":[{"source":"PubMed","id":"22814378","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI4 |
Number of Residues | 16 |
Details | Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"PubMed","id":"12872131","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1dbt |
Chain | Residue | Details |
A | ASP91 | |
A | LYS93 |
site_id | CSA2 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1dbt |
Chain | Residue | Details |
B | ASP91 | |
B | LYS93 |
site_id | CSA3 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1dbt |
Chain | Residue | Details |
C | ASP91 | |
C | LYS93 |
site_id | CSA4 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1dbt |
Chain | Residue | Details |
D | ASP91 | |
D | LYS93 |
site_id | CSA5 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1dbt |
Chain | Residue | Details |
A | LYS59 | |
A | ASP96 | |
A | ASP91 | |
A | LYS93 |
site_id | CSA6 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1dbt |
Chain | Residue | Details |
B | LYS59 | |
B | ASP96 | |
B | ASP91 | |
B | LYS93 |
site_id | CSA7 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1dbt |
Chain | Residue | Details |
C | LYS59 | |
C | ASP96 | |
C | ASP91 | |
C | LYS93 |
site_id | CSA8 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1dbt |
Chain | Residue | Details |
D | LYS59 | |
D | ASP96 | |
D | ASP91 | |
D | LYS93 |