5T3O
Crystal structure of the Phosphorybosylpyrophosphate synthetase II from Thermus thermophilus
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000287 | molecular_function | magnesium ion binding |
| A | 0002189 | cellular_component | ribose phosphate diphosphokinase complex |
| A | 0004749 | molecular_function | ribose phosphate diphosphokinase activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0006015 | biological_process | 5-phosphoribose 1-diphosphate biosynthetic process |
| A | 0006164 | biological_process | purine nucleotide biosynthetic process |
| A | 0009165 | biological_process | nucleotide biosynthetic process |
| B | 0000287 | molecular_function | magnesium ion binding |
| B | 0002189 | cellular_component | ribose phosphate diphosphokinase complex |
| B | 0004749 | molecular_function | ribose phosphate diphosphokinase activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0006015 | biological_process | 5-phosphoribose 1-diphosphate biosynthetic process |
| B | 0006164 | biological_process | purine nucleotide biosynthetic process |
| B | 0009165 | biological_process | nucleotide biosynthetic process |
| C | 0000287 | molecular_function | magnesium ion binding |
| C | 0002189 | cellular_component | ribose phosphate diphosphokinase complex |
| C | 0004749 | molecular_function | ribose phosphate diphosphokinase activity |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0006015 | biological_process | 5-phosphoribose 1-diphosphate biosynthetic process |
| C | 0006164 | biological_process | purine nucleotide biosynthetic process |
| C | 0009165 | biological_process | nucleotide biosynthetic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 11 |
| Details | binding site for residue ADP A 401 |
| Chain | Residue |
| A | SER94 |
| C | ASN38 |
| C | ASN40 |
| A | ARG97 |
| A | SER98 |
| A | LYS100 |
| A | ASP102 |
| A | HIS131 |
| A | ASP171 |
| A | ARG196 |
| C | PHE36 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | binding site for residue SO4 A 402 |
| Chain | Residue |
| A | ARG105 |
| A | SER304 |
| A | VAL305 |
| A | SER306 |
| C | SER48 |
| C | ARG50 |
| C | HOH519 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | binding site for residue SO4 A 403 |
| Chain | Residue |
| A | SER224 |
| A | THR225 |
| A | ALA226 |
| A | GLY227 |
| A | SER228 |
| site_id | AC4 |
| Number of Residues | 12 |
| Details | binding site for residue ADP B 401 |
| Chain | Residue |
| B | PHE36 |
| B | ASN38 |
| B | ASN40 |
| B | ARG97 |
| B | SER98 |
| B | LYS100 |
| B | ASP102 |
| B | HIS131 |
| B | ASP171 |
| B | ARG196 |
| B | HOH552 |
| B | HOH585 |
| site_id | AC5 |
| Number of Residues | 8 |
| Details | binding site for residue SO4 B 402 |
| Chain | Residue |
| A | SER48 |
| A | ARG50 |
| B | SER304 |
| B | VAL305 |
| B | SER306 |
| B | HOH529 |
| B | HOH575 |
| C | ARG105 |
| site_id | AC6 |
| Number of Residues | 9 |
| Details | binding site for residue SO4 B 403 |
| Chain | Residue |
| B | ARG196 |
| B | SER224 |
| B | THR225 |
| B | ALA226 |
| B | GLY227 |
| B | SER228 |
| B | HOH515 |
| B | HOH556 |
| B | HOH567 |
| site_id | AC7 |
| Number of Residues | 8 |
| Details | binding site for residue ADP C 401 |
| Chain | Residue |
| A | PHE36 |
| A | ASN38 |
| A | ASN40 |
| C | ARG97 |
| C | SER98 |
| C | LYS100 |
| C | ASP102 |
| C | HIS131 |
| site_id | AC8 |
| Number of Residues | 8 |
| Details | binding site for residue SO4 C 402 |
| Chain | Residue |
| B | SER48 |
| B | ARG50 |
| B | ARG105 |
| B | HOH524 |
| C | SER304 |
| C | VAL305 |
| C | SER306 |
| C | HOH540 |
| site_id | AC9 |
| Number of Residues | 7 |
| Details | binding site for residue SO4 C 403 |
| Chain | Residue |
| C | SER224 |
| C | THR225 |
| C | ALA226 |
| C | GLY227 |
| C | SER228 |
| C | HOH520 |
| C | HOH529 |
