6ZTC
CRYSTAL STRUCTURE OF PROSTAGLANDIN D2 SYNTHASE IN COMPLEX WITH FRAGMENT 1A AT 1.84A RESOLUTION.
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 | 0005515 | molecular_function | protein binding |
| A | 0005654 | cellular_component | nucleoplasm |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0006693 | biological_process | prostaglandin metabolic process |
| A | 0007165 | biological_process | signal transduction |
| A | 0007626 | biological_process | locomotory behavior |
| A | 0016740 | molecular_function | transferase activity |
| A | 0016853 | molecular_function | isomerase activity |
| A | 0042803 | molecular_function | protein homodimerization activity |
| A | 0043231 | cellular_component | intracellular membrane-bounded organelle |
| A | 0046872 | molecular_function | metal ion binding |
| 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 | 0005515 | molecular_function | protein binding |
| B | 0005654 | cellular_component | nucleoplasm |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0006693 | biological_process | prostaglandin metabolic process |
| B | 0007165 | biological_process | signal transduction |
| B | 0007626 | biological_process | locomotory behavior |
| B | 0016740 | molecular_function | transferase activity |
| B | 0016853 | molecular_function | isomerase activity |
| B | 0042803 | molecular_function | protein homodimerization activity |
| B | 0043231 | cellular_component | intracellular membrane-bounded organelle |
| B | 0046872 | molecular_function | metal ion binding |
| B | 2000255 | biological_process | negative regulation of male germ cell proliferation |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 17 |
| Details | binding site for residue GSH A 201 |
| Chain | Residue |
| A | TYR8 |
| A | HOH324 |
| A | HOH340 |
| A | HOH374 |
| A | HOH386 |
| A | HOH421 |
| A | HOH424 |
| A | HOH450 |
| B | ASP97 |
| A | ARG14 |
| A | TRP39 |
| A | LYS43 |
| A | LYS50 |
| A | ILE51 |
| A | GLN63 |
| A | SER64 |
| A | QPN203 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | binding site for residue MG A 202 |
| Chain | Residue |
| A | HOH351 |
| A | HOH385 |
| A | HOH442 |
| B | HOH340 |
| B | HOH352 |
| B | HOH392 |
| site_id | AC3 |
| Number of Residues | 10 |
| Details | binding site for residue QPN A 203 |
| Chain | Residue |
| A | GLY13 |
| A | ARG14 |
| A | ASP96 |
| A | MET99 |
| A | SER100 |
| A | TRP104 |
| A | TYR152 |
| A | LEU199 |
| A | GSH201 |
| A | HOH355 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | binding site for residue GOL A 204 |
| Chain | Residue |
| A | GLU82 |
| A | HOH359 |
| B | TYR70 |
| B | LYS73 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | binding site for residue GOL A 205 |
| Chain | Residue |
| A | GLU55 |
| A | THR60 |
| A | HOH481 |
| site_id | AC6 |
| Number of Residues | 16 |
| 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 | GLN63 |
| B | SER64 |
| B | QPN202 |
| B | HOH328 |
| B | HOH346 |
| B | HOH397 |
| B | HOH404 |
| B | HOH449 |
| B | HOH502 |
| site_id | AC7 |
| Number of Residues | 13 |
| Details | binding site for residue QPN B 202 |
| Chain | Residue |
| B | TYR8 |
| B | MET11 |
| B | GLY13 |
| B | ARG14 |
| B | ASP96 |
| B | MET99 |
| B | SER100 |
| B | TRP104 |
| B | TYR152 |
| B | THR159 |
| B | LEU199 |
| B | GSH201 |
| B | HOH332 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | binding site for residue GOL B 203 |
| Chain | Residue |
| B | LYS112 |
| B | HOH307 |
| B | HOH316 |
| B | HOH487 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 10 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:12627223, ECO:0000269|PubMed:15113825, ECO:0000269|PubMed:16547010, ECO:0000269|PubMed:18341273, ECO:0000269|PubMed:19939518 |
| Chain | Residue | Details |
| A | TYR8 | |
| B | GLN63 | |
| A | ARG14 | |
| A | TRP39 | |
| A | GLY49 | |
| A | GLN63 | |
| B | TYR8 | |
| B | ARG14 | |
| B | TRP39 | |
| B | GLY49 |
