3S9Y
Crystal Structure of P. falciparum orotidine 5'-monophosphate decarboxylase complexed with 5-fluoro-6-amino-UMP in space group P21, produced from 5-fluoro-6-azido-UMP
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004590 | molecular_function | orotidine-5'-phosphate decarboxylase activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0006207 | biological_process | 'de novo' pyrimidine nucleobase biosynthetic process |
| A | 0006221 | biological_process | pyrimidine nucleotide 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 | 0005515 | molecular_function | protein binding |
| B | 0006207 | biological_process | 'de novo' pyrimidine nucleobase biosynthetic process |
| B | 0006221 | biological_process | pyrimidine nucleotide 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 | 0005515 | molecular_function | protein binding |
| C | 0006207 | biological_process | 'de novo' pyrimidine nucleobase biosynthetic process |
| C | 0006221 | biological_process | pyrimidine nucleotide 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 | 0005515 | molecular_function | protein binding |
| D | 0006207 | biological_process | 'de novo' pyrimidine nucleobase biosynthetic process |
| D | 0006221 | biological_process | pyrimidine nucleotide 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 | 22 |
| Details | BINDING SITE FOR RESIDUE FNU A 324 |
| Chain | Residue |
| A | ASP23 |
| A | PRO264 |
| A | GLN269 |
| A | GLY293 |
| A | ARG294 |
| A | HOH329 |
| A | HOH330 |
| A | HOH334 |
| A | HOH338 |
| A | HOH339 |
| A | HOH378 |
| A | LYS102 |
| B | ASP141 |
| B | ILE142 |
| B | THR145 |
| A | ASN104 |
| A | ASP136 |
| A | LYS138 |
| A | LEU191 |
| A | THR194 |
| A | THR195 |
| A | VAL240 |
| site_id | AC2 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE FNU B 324 |
| Chain | Residue |
| A | ASP141 |
| A | ILE142 |
| A | THR145 |
| B | ASP23 |
| B | LYS102 |
| B | ASN104 |
| B | ASP136 |
| B | LYS138 |
| B | LEU191 |
| B | THR194 |
| B | THR195 |
| B | VAL240 |
| B | PRO264 |
| B | GLN269 |
| B | GLY293 |
| B | ARG294 |
| B | HOH326 |
| B | HOH341 |
| B | HOH349 |
| B | HOH353 |
| B | HOH355 |
| B | HOH385 |
| site_id | AC3 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE SO4 B 2000 |
| Chain | Residue |
| B | LYS147 |
| B | ARG150 |
| B | ASP179 |
| B | GLU180 |
| B | GLU181 |
| B | HOH415 |
| B | HOH678 |
| B | HOH972 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE PGE B 3000 |
| Chain | Residue |
| B | ASN299 |
| B | TYR301 |
| C | ASN299 |
| C | TYR301 |
| C | ALA305 |
| C | MET308 |
| site_id | AC5 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE PEG B 3001 |
| Chain | Residue |
| A | ILE142 |
| A | GLY143 |
| A | ASN171 |
| A | HOH404 |
| B | THR195 |
| B | ASN196 |
| B | PRO197 |
| B | GLN269 |
| B | HOH467 |
| B | HOH468 |
| B | HOH605 |
| site_id | AC6 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE P6G B 3003 |
| Chain | Residue |
| B | TYR251 |
| B | TYR255 |
| B | HOH466 |
| B | HOH559 |
| B | HOH1094 |
| C | LYS174 |
| C | MET224 |
| C | TYR227 |
| C | HOH620 |
| D | HOH870 |
| site_id | AC7 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE FNU C 324 |
| Chain | Residue |
| D | ILE142 |
| D | THR145 |
| C | ASP23 |
| C | LYS102 |
| C | ASN104 |
| C | ASP136 |
| C | LYS138 |
| C | LEU191 |
| C | THR194 |
| C | THR195 |
| C | VAL240 |
| C | PRO264 |
| C | GLN269 |
| C | GLY293 |
| C | ARG294 |
| C | HOH325 |
| C | HOH327 |
| C | HOH335 |
| C | HOH346 |
| C | HOH352 |
| C | HOH353 |
| D | ASP141 |
| site_id | AC8 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE P6G C 3002 |
| Chain | Residue |
| A | ASN205 |
| B | LYS174 |
| B | MET224 |
| B | TYR227 |
| C | ASP209 |
| C | TYR251 |
| C | TYR255 |
| C | HOH386 |
| C | HOH416 |
| C | HOH657 |
| C | HOH714 |
| C | HOH767 |
| C | HOH1078 |
| site_id | AC9 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE FNU D 324 |
| Chain | Residue |
| C | ASP141 |
| C | ILE142 |
| C | THR145 |
| D | ASP23 |
| D | LYS102 |
| D | ASN104 |
| D | ASP136 |
| D | LYS138 |
| D | LEU191 |
| D | THR194 |
| D | THR195 |
| D | VAL240 |
| D | PRO264 |
| D | GLN269 |
| D | GLY293 |
| D | ARG294 |
| D | HOH325 |
| D | HOH328 |
| D | HOH330 |
| D | HOH334 |
| D | HOH335 |
| D | HOH346 |
Functional Information from PROSITE/UniProt
| site_id | PS00156 |
| Number of Residues | 14 |
| Details | OMPDECASE Orotidine 5'-phosphate decarboxylase active site. TIlDmKinDIGnTV |
| Chain | Residue | Details |
| A | THR133-VAL146 |
