3RU6
1.8 Angstrom resolution crystal structure of orotidine 5'-phosphate decarboxylase (pyrF) from Campylobacter jejuni subsp. jejuni NCTC 11168
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 | 3 |
Details | BINDING SITE FOR RESIDUE CL A 280 |
Chain | Residue |
A | LYS91 |
D | ASN123 |
D | HOH352 |
site_id | AC2 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE IOD A 281 |
Chain | Residue |
A | LEU59 |
D | LEU59 |
site_id | AC3 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE IOD A 282 |
Chain | Residue |
A | LYS103 |
A | ARG207 |
site_id | AC4 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE IOD A 284 |
Chain | Residue |
A | GLY175 |
site_id | AC5 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE IOD A 285 |
Chain | Residue |
A | THR117 |
site_id | AC6 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE IOD A 286 |
Chain | Residue |
A | ARG100 |
A | LYS103 |
site_id | AC7 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE IOD A 287 |
Chain | Residue |
A | PHE179 |
site_id | AC8 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE IOD B 280 |
Chain | Residue |
B | THR117 |
site_id | AC9 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE IOD B 281 |
Chain | Residue |
B | PHE179 |
site_id | BC1 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE IOD B 282 |
Chain | Residue |
B | ARG100 |
B | LYS103 |
B | ARG207 |
site_id | BC2 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE IOD B 283 |
Chain | Residue |
B | LEU59 |
C | LEU59 |
site_id | BC3 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE IOD B 284 |
Chain | Residue |
B | LYS103 |
B | ARG207 |
site_id | BC4 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE IOD B 285 |
Chain | Residue |
B | GLY175 |
site_id | BC5 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE IOD B 286 |
Chain | Residue |
B | ARG196 |
site_id | BC6 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE IOD B 287 |
Chain | Residue |
B | LYS12 |
B | LYS42 |
B | GLU46 |
site_id | BC7 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE CL C 280 |
Chain | Residue |
B | ASN123 |
B | HOH292 |
C | LYS91 |
site_id | BC8 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE CL C 281 |
Chain | Residue |
B | GLY90 |
B | LYS91 |
C | ASN123 |
C | SER126 |
C | HOH303 |
site_id | BC9 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE IOD C 282 |
Chain | Residue |
C | THR117 |
C | HOH366 |
site_id | CC1 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE IOD C 283 |
Chain | Residue |
C | GLY175 |
site_id | CC2 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE IOD C 286 |
Chain | Residue |
C | ARG100 |
C | LYS103 |
site_id | CC3 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE IOD C 287 |
Chain | Residue |
C | LYS12 |
site_id | CC4 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE CL D 280 |
Chain | Residue |
D | ALA193 |
D | ARG196 |
D | LYS225 |
site_id | CC5 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE IOD D 281 |
Chain | Residue |
D | GLY175 |
site_id | CC6 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE IOD D 282 |
Chain | Residue |
D | ARG100 |
D | LYS103 |
site_id | CC7 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE IOD D 283 |
Chain | Residue |
D | ARG177 |
D | PHE179 |
site_id | CC8 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE IOD D 284 |
Chain | Residue |
D | LYS103 |
D | ARG177 |
site_id | CC9 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE IOD D 285 |
Chain | Residue |
D | THR117 |
D | HOH342 |
Functional Information from PROSITE/UniProt
site_id | PS00156 |
Number of Residues | 14 |
Details | OMPDECASE Orotidine 5'-phosphate decarboxylase active site. IFlDlKfhDIPnTM |
Chain | Residue | Details |
A | ILE55-MET68 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 4 |
Details | ACT_SITE: Proton donor => ECO:0000255|HAMAP-Rule:MF_01200 |
Chain | Residue | Details |
A | LYS60 | |
B | LYS60 | |
C | LYS60 | |
D | LYS60 |
site_id | SWS_FT_FI2 |
Number of Residues | 32 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01200 |
Chain | Residue | Details |
A | ASP8 | |
B | LYS30 | |
B | ASP58 | |
B | THR117 | |
B | ARG177 | |
B | GLN186 | |
B | GLY206 | |
B | ARG207 | |
C | ASP8 | |
C | LYS30 | |
C | ASP58 | |
A | LYS30 | |
C | THR117 | |
C | ARG177 | |
C | GLN186 | |
C | GLY206 | |
C | ARG207 | |
D | ASP8 | |
D | LYS30 | |
D | ASP58 | |
D | THR117 | |
D | ARG177 | |
A | ASP58 | |
D | GLN186 | |
D | GLY206 | |
D | ARG207 | |
A | THR117 | |
A | ARG177 | |
A | GLN186 | |
A | GLY206 | |
A | ARG207 | |
B | ASP8 |