5Y9Z
Crystal structure of rat hematopoietic prostaglandin D synthase
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 | 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 | 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 | 16 |
| Details | binding site for residue GSH A 201 |
| Chain | Residue |
| A | TYR8 |
| A | HOH367 |
| A | HOH406 |
| A | HOH415 |
| A | HOH424 |
| A | HOH445 |
| A | HOH475 |
| B | ASP97 |
| A | ARG14 |
| A | TRP39 |
| A | LYS43 |
| A | LYS50 |
| A | ILE51 |
| A | GLN63 |
| A | SER64 |
| A | HOH335 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | binding site for residue MG A 202 |
| Chain | Residue |
| A | HOH321 |
| A | HOH341 |
| A | HOH353 |
| B | HOH341 |
| B | HOH343 |
| B | HOH349 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | binding site for residue MG A 203 |
| Chain | Residue |
| A | HOH381 |
| A | HOH386 |
| A | HOH390 |
| A | HOH513 |
| A | HOH532 |
| A | HOH563 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | binding site for residue DIO A 204 |
| Chain | Residue |
| A | GLY13 |
| A | DIO205 |
| A | HOH515 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | binding site for residue DIO A 205 |
| Chain | Residue |
| A | MET99 |
| A | TYR152 |
| A | ILE155 |
| A | DIO204 |
| A | HOH389 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | binding site for residue EDO A 206 |
| Chain | Residue |
| A | ASN144 |
| A | GOL209 |
| B | LYS41 |
| B | ILE42 |
| B | THR45 |
| B | HOH500 |
| site_id | AC7 |
| Number of Residues | 7 |
| Details | binding site for residue EDO A 207 |
| Chain | Residue |
| A | ASN10 |
| A | ARG33 |
| A | GLU35 |
| A | HOH325 |
| A | HOH355 |
| B | ASN10 |
| B | GLU35 |
| site_id | AC8 |
| Number of Residues | 8 |
| Details | binding site for residue EDO A 208 |
| Chain | Residue |
| A | ALA183 |
| A | PRO185 |
| A | HOH317 |
| A | HOH332 |
| A | HOH402 |
| A | HOH567 |
| A | HOH570 |
| B | HOH377 |
| site_id | AC9 |
| Number of Residues | 11 |
| Details | binding site for residue GOL A 209 |
| Chain | Residue |
| A | GLU139 |
| A | TRP140 |
| A | ASN144 |
| A | TYR145 |
| A | EDO206 |
| A | HOH319 |
| A | HOH338 |
| A | HOH443 |
| A | HOH463 |
| A | HOH467 |
| B | THR45 |
| site_id | AD1 |
| 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 | GLN63 |
| B | SER64 |
| B | HOH325 |
| B | HOH373 |
| B | HOH383 |
| B | HOH398 |
| B | HOH408 |
| site_id | AD2 |
| Number of Residues | 5 |
| Details | binding site for residue DIO B 202 |
| Chain | Residue |
| B | MET99 |
| B | TYR152 |
| B | ILE155 |
| B | DIO203 |
| B | HOH372 |
| site_id | AD3 |
| Number of Residues | 3 |
| Details | binding site for residue DIO B 203 |
| Chain | Residue |
| B | GLY13 |
| B | DIO202 |
| B | HOH502 |
| site_id | AD4 |
| Number of Residues | 6 |
| Details | binding site for residue PGE B 204 |
| Chain | Residue |
| A | LEU83 |
| A | ASN179 |
| B | VAL56 |
| B | GLU57 |
| B | HOH323 |
| B | HOH450 |
| site_id | AD5 |
| Number of Residues | 2 |
| Details | binding site for residue PGE B 205 |
| Chain | Residue |
| B | TYR24 |
| B | LEU25 |
| site_id | AD6 |
| Number of Residues | 8 |
| Details | binding site for residue EDO B 206 |
| Chain | Residue |
| A | ASP166 |
| A | LEU167 |
| A | TYR171 |
| A | HOH468 |
| A | HOH478 |
| B | VAL175 |
| B | ASN179 |
| A | PRO125 |
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 |
