3N3Y
Crystal structure of Thymidylate Synthase X (ThyX) from Helicobacter pylori with FAD and dUMP at 2.31A resolution
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0004799 | molecular_function | thymidylate synthase activity |
| A | 0006231 | biological_process | dTMP biosynthetic process |
| A | 0006235 | biological_process | dTTP biosynthetic process |
| A | 0008168 | molecular_function | methyltransferase activity |
| A | 0009165 | biological_process | nucleotide biosynthetic process |
| A | 0032259 | biological_process | methylation |
| A | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| A | 0050797 | molecular_function | thymidylate synthase (FAD) activity |
| A | 0070402 | molecular_function | NADPH binding |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0004799 | molecular_function | thymidylate synthase activity |
| B | 0006231 | biological_process | dTMP biosynthetic process |
| B | 0006235 | biological_process | dTTP biosynthetic process |
| B | 0008168 | molecular_function | methyltransferase activity |
| B | 0009165 | biological_process | nucleotide biosynthetic process |
| B | 0032259 | biological_process | methylation |
| B | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| B | 0050797 | molecular_function | thymidylate synthase (FAD) activity |
| B | 0070402 | molecular_function | NADPH binding |
| C | 0000166 | molecular_function | nucleotide binding |
| C | 0004799 | molecular_function | thymidylate synthase activity |
| C | 0006231 | biological_process | dTMP biosynthetic process |
| C | 0006235 | biological_process | dTTP biosynthetic process |
| C | 0008168 | molecular_function | methyltransferase activity |
| C | 0009165 | biological_process | nucleotide biosynthetic process |
| C | 0032259 | biological_process | methylation |
| C | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| C | 0050797 | molecular_function | thymidylate synthase (FAD) activity |
| C | 0070402 | molecular_function | NADPH binding |
| D | 0000166 | molecular_function | nucleotide binding |
| D | 0004799 | molecular_function | thymidylate synthase activity |
| D | 0006231 | biological_process | dTMP biosynthetic process |
| D | 0006235 | biological_process | dTTP biosynthetic process |
| D | 0008168 | molecular_function | methyltransferase activity |
| D | 0009165 | biological_process | nucleotide biosynthetic process |
| D | 0032259 | biological_process | methylation |
| D | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| D | 0050797 | molecular_function | thymidylate synthase (FAD) activity |
| D | 0070402 | molecular_function | NADPH binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE UMP B 301 |
| Chain | Residue |
| A | ARG66 |
| B | ARG174 |
| B | FAD209 |
| B | HOH214 |
| B | HOH216 |
| B | HOH224 |
| A | VAL82 |
| A | LYS83 |
| A | SER84 |
| A | SER85 |
| A | ARG86 |
| A | LYS147 |
| B | GLU71 |
| B | ARG74 |
| site_id | AC2 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE UMP D 302 |
| Chain | Residue |
| C | GLU71 |
| C | ARG74 |
| C | ARG174 |
| C | HOH221 |
| C | FAD302 |
| D | ARG66 |
| D | LYS83 |
| D | SER84 |
| D | SER85 |
| D | ARG86 |
| D | LYS147 |
| D | HOH210 |
| D | HOH228 |
| site_id | AC3 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE UMP C 303 |
| Chain | Residue |
| C | ARG66 |
| C | LYS83 |
| C | SER84 |
| C | SER85 |
| C | ARG86 |
| C | LYS147 |
| D | GLU71 |
| D | ARG74 |
| D | ARG174 |
| D | HOH209 |
| D | HOH211 |
| D | HOH239 |
| D | FAD303 |
| site_id | AC4 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE UMP B 304 |
| Chain | Residue |
| A | GLU71 |
| A | ARG74 |
| A | ARG174 |
| A | HOH218 |
| A | FAD304 |
| B | ARG66 |
| B | VAL82 |
| B | LYS83 |
| B | SER84 |
| B | SER85 |
| B | ARG86 |
| B | LYS147 |
| B | HOH210 |
| B | HOH211 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE UMP A 305 |
| Chain | Residue |
| A | HIS7 |
| A | TYR8 |
| A | PRO10 |
| site_id | AC6 |
| Number of Residues | 23 |
| Details | BINDING SITE FOR RESIDUE FAD B 209 |
| Chain | Residue |
| A | SER81 |
| A | VAL82 |
| A | SER84 |
| A | HOH224 |
| B | ARG74 |
| B | HIS75 |
| B | ARG76 |
| B | ILE77 |
| B | ASN169 |
| B | ARG174 |
| B | HOH212 |
| B | HOH233 |
| B | UMP301 |
| D | CYS21 |
| D | PHE46 |
| D | ARG47 |
| D | SER50 |
| D | GLU53 |
| D | ILE77 |
| D | ASN163 |
| D | ARG165 |
| D | SER166 |
| D | FAD303 |
| site_id | AC7 |
| Number of Residues | 25 |
| Details | BINDING SITE FOR RESIDUE FAD C 302 |
| Chain | Residue |
| C | HOH220 |
| C | HOH224 |
| D | SER81 |
| D | VAL82 |
| D | SER84 |
| D | UMP302 |
| A | CYS21 |
| A | PHE46 |
| A | ARG47 |
| A | SER50 |
| A | GLU53 |
| A | ILE77 |
| A | ASN163 |
| A | ARG165 |
| A | HOH234 |
| A | FAD304 |
| C | ARG74 |
| C | HIS75 |
| C | ARG76 |
| C | ILE77 |
| C | ASN169 |
| C | ARG174 |
| C | LYS178 |
| C | HOH213 |
| C | HOH215 |
| site_id | AC8 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE FAD D 303 |
| Chain | Residue |
| B | PHE46 |
| B | ARG47 |
| B | SER50 |
| B | GLU53 |
| B | ILE77 |
| B | ASN163 |
| B | ARG165 |
| B | FAD209 |
| B | HOH247 |
| C | SER81 |
| C | VAL82 |
| C | SER84 |
| C | UMP303 |
| D | ARG74 |
| D | HIS75 |
| D | ARG76 |
| D | ILE77 |
| D | ASN169 |
| D | ARG174 |
| D | LYS178 |
| D | HOH214 |
| D | HOH229 |
| site_id | AC9 |
| Number of Residues | 23 |
| Details | BINDING SITE FOR RESIDUE FAD A 304 |
| Chain | Residue |
| A | ARG74 |
| A | HIS75 |
| A | ARG76 |
| A | ILE77 |
| A | ASN169 |
| A | ARG174 |
| A | HOH226 |
| A | HOH239 |
| A | HOH242 |
| B | SER81 |
| B | VAL82 |
| B | SER84 |
| B | TYR87 |
| B | UMP304 |
| C | CYS21 |
| C | PHE46 |
| C | ARG47 |
| C | SER50 |
| C | GLU53 |
| C | ILE77 |
| C | ASN163 |
| C | ARG165 |
| C | FAD302 |
