3N3M
Crystal structure of Plasmodium falciparum orotidine 5'-monophosphate decarboxylase complexed with 6-amino-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 | 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 | 0016831 | molecular_function | carboxy-lyase activity |
B | 0044205 | biological_process | 'de novo' UMP biosynthetic process |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE PO4 B 3000 |
Chain | Residue |
B | LYS147 |
B | ARG150 |
B | ASP179 |
B | GLU180 |
B | GLU181 |
B | HOH481 |
B | HOH530 |
site_id | AC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE PGE A 4000 |
Chain | Residue |
A | MET308 |
A | TYR309 |
A | GLN312 |
A | ASN299 |
A | PRO300 |
site_id | AC3 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE PGE A 4001 |
Chain | Residue |
A | LYS174 |
A | LYS211 |
A | VAL215 |
A | MET224 |
A | TYR227 |
A | TYR251 |
A | TYR255 |
A | HOH557 |
site_id | AC4 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE EDO B 4002 |
Chain | Residue |
A | ASN196 |
A | PRO197 |
B | ILE142 |
B | GLY143 |
B | ASN171 |
B | HOH376 |
B | HOH379 |
B | HOH410 |
site_id | AC5 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE EDO A 4003 |
Chain | Residue |
A | ILE142 |
A | GLY143 |
A | ASN171 |
A | HOH352 |
A | HOH449 |
B | ASN196 |
B | PRO197 |
B | HOH496 |
site_id | AC6 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE EDO B 4004 |
Chain | Residue |
B | TYR178 |
B | GLU180 |
B | ASP272 |
B | HIS274 |
B | LYS275 |
B | HOH531 |
site_id | AC7 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE EDO B 4005 |
Chain | Residue |
B | PHE123 |
B | TYR127 |
B | THR133 |
B | LEU157 |
B | LYS158 |
B | SER159 |
B | ASP160 |
B | HOH428 |
B | HOH443 |
site_id | AC8 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE GOL A 5000 |
Chain | Residue |
A | MET1 |
A | PHE3 |
A | ASN40 |
A | ASP160 |
A | GLU235 |
A | HOH389 |
A | HOH535 |
A | HOH640 |
site_id | AC9 |
Number of Residues | 21 |
Details | BINDING SITE FOR RESIDUE NUP A 2000 |
Chain | Residue |
A | ASP23 |
A | LYS102 |
A | ASN104 |
A | ASP136 |
A | LYS138 |
A | THR194 |
A | THR195 |
A | PRO264 |
A | GLN269 |
A | ASN291 |
A | GLY293 |
A | ARG294 |
A | HOH330 |
A | HOH332 |
A | HOH335 |
A | HOH340 |
A | HOH346 |
A | HOH566 |
B | ASP141 |
B | ILE142 |
B | THR145 |
site_id | BC1 |
Number of Residues | 20 |
Details | BINDING SITE FOR RESIDUE NUP B 2001 |
Chain | Residue |
B | HOH580 |
A | ASP141 |
A | ILE142 |
A | THR145 |
B | ASP23 |
B | LYS102 |
B | ASN104 |
B | ASP136 |
B | LYS138 |
B | THR194 |
B | THR195 |
B | PRO264 |
B | GLN269 |
B | GLY293 |
B | ARG294 |
B | HOH337 |
B | HOH341 |
B | HOH345 |
B | HOH347 |
B | HOH383 |
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 |