6N69
rat hPGDS complexed with a quinoline
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000287 | molecular_function | magnesium ion binding |
| A | 0001516 | biological_process | prostaglandin biosynthetic process |
| A | 0004364 | molecular_function | glutathione transferase activity |
| A | 0004667 | molecular_function | prostaglandin-D synthase activity |
| A | 0005509 | molecular_function | calcium ion binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0006693 | biological_process | prostaglandin metabolic process |
| A | 0009624 | biological_process | response to nematode |
| A | 0010269 | biological_process | response to selenium ion |
| A | 0016740 | molecular_function | transferase activity |
| A | 0016853 | molecular_function | isomerase activity |
| A | 0042803 | molecular_function | protein homodimerization activity |
| A | 2000255 | biological_process | negative regulation of male germ cell proliferation |
| B | 0000287 | molecular_function | magnesium ion binding |
| B | 0001516 | biological_process | prostaglandin biosynthetic process |
| B | 0004364 | molecular_function | glutathione transferase activity |
| B | 0004667 | molecular_function | prostaglandin-D synthase activity |
| B | 0005509 | molecular_function | calcium ion binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0006693 | biological_process | prostaglandin metabolic process |
| B | 0009624 | biological_process | response to nematode |
| B | 0010269 | biological_process | response to selenium ion |
| B | 0016740 | molecular_function | transferase activity |
| B | 0016853 | molecular_function | isomerase activity |
| B | 0042803 | molecular_function | protein homodimerization activity |
| B | 2000255 | biological_process | negative regulation of male germ cell proliferation |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 14 |
| Details | binding site for residue GSH A 201 |
| Chain | Residue |
| A | TYR8 |
| A | HOH330 |
| A | HOH336 |
| A | HOH380 |
| A | HOH404 |
| B | ASP97 |
| A | ARG14 |
| A | TRP39 |
| A | LYS43 |
| A | LYS50 |
| A | ILE51 |
| A | PRO52 |
| A | GLN63 |
| A | SER64 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | binding site for residue KDV A 202 |
| Chain | Residue |
| A | MET11 |
| A | GLY13 |
| A | ARG14 |
| A | MET99 |
| A | TRP104 |
| A | TYR152 |
| site_id | AC3 |
| Number of Residues | 14 |
| Details | binding site for residue GSH B 201 |
| Chain | Residue |
| A | ASP97 |
| B | TYR8 |
| B | ARG14 |
| B | TRP39 |
| B | LYS43 |
| B | LYS50 |
| B | ILE51 |
| B | PRO52 |
| B | GLN63 |
| B | SER64 |
| B | HOH325 |
| B | HOH365 |
| B | HOH366 |
| B | HOH399 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | binding site for residue KDV B 202 |
| Chain | Residue |
| B | GLY13 |
| B | ARG14 |
| B | MET99 |
| B | TRP104 |
| B | HOH302 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 10 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:9323136 |
| Chain | Residue | Details |
| A | TYR8 | |
| B | GLN63 | |
| A | ARG14 | |
| A | TRP39 | |
| A | GLY49 | |
| A | GLN63 | |
| B | TYR8 | |
| B | ARG14 | |
| B | TRP39 | |
| B | GLY49 |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 3 |
| Details | M-CSA 719 |
| Chain | Residue | Details |
| A | TYR8 | electrostatic stabiliser, modifies pKa |
| A | ARG14 | electrostatic stabiliser |
| A | TRP104 | electrostatic stabiliser, steric role |
| site_id | MCSA2 |
| Number of Residues | 3 |
| Details | M-CSA 719 |
| Chain | Residue | Details |
| B | TYR8 | electrostatic stabiliser, modifies pKa |
| B | ARG14 | electrostatic stabiliser |
| B | TRP104 | electrostatic stabiliser, steric role |
