1PD2
CRYSTAL STRUCTURE OF HEMATOPOIETIC PROSTAGLANDIN D SYNTHASE COMPLEX WITH GLUTATHIONE
Functional Information from GO Data
Chain | GOid | namespace | contents |
1 | 0000287 | molecular_function | magnesium ion binding |
1 | 0001516 | biological_process | prostaglandin biosynthetic process |
1 | 0004364 | molecular_function | glutathione transferase activity |
1 | 0004667 | molecular_function | prostaglandin-D synthase activity |
1 | 0005509 | molecular_function | calcium ion binding |
1 | 0005737 | cellular_component | cytoplasm |
1 | 0006693 | biological_process | prostaglandin metabolic process |
1 | 0009624 | biological_process | response to nematode |
1 | 0010269 | biological_process | response to selenium ion |
1 | 0016740 | molecular_function | transferase activity |
1 | 0016853 | molecular_function | isomerase activity |
1 | 0042803 | molecular_function | protein homodimerization activity |
1 | 2000255 | biological_process | negative regulation of male germ cell proliferation |
2 | 0000287 | molecular_function | magnesium ion binding |
2 | 0001516 | biological_process | prostaglandin biosynthetic process |
2 | 0004364 | molecular_function | glutathione transferase activity |
2 | 0004667 | molecular_function | prostaglandin-D synthase activity |
2 | 0005509 | molecular_function | calcium ion binding |
2 | 0005737 | cellular_component | cytoplasm |
2 | 0006693 | biological_process | prostaglandin metabolic process |
2 | 0009624 | biological_process | response to nematode |
2 | 0010269 | biological_process | response to selenium ion |
2 | 0016740 | molecular_function | transferase activity |
2 | 0016853 | molecular_function | isomerase activity |
2 | 0042803 | molecular_function | protein homodimerization activity |
2 | 2000255 | biological_process | negative regulation of male germ cell proliferation |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE GSH 1 301 |
Chain | Residue |
1 | TYR8 |
2 | ASP97 |
1 | ARG14 |
1 | TRP39 |
1 | LYS43 |
1 | LYS50 |
1 | ILE51 |
1 | GLN63 |
1 | SER64 |
1 | HOH320 |
site_id | AC2 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE GSH 2 302 |
Chain | Residue |
1 | ASP97 |
2 | TYR8 |
2 | ARG14 |
2 | TRP39 |
2 | LYS43 |
2 | LYS50 |
2 | ILE51 |
2 | GLN63 |
2 | SER64 |
2 | HOH311 |
2 | HOH323 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 10 |
Details | BINDING: BINDING => ECO:0000269|PubMed:9323136 |
Chain | Residue | Details |
1 | TYR8 | |
2 | GLN63 | |
1 | ARG14 | |
1 | TRP39 | |
1 | GLY49 | |
1 | GLN63 | |
2 | TYR8 | |
2 | ARG14 | |
2 | TRP39 | |
2 | GLY49 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 3 |
Details |
Chain | Residue | Details |
1 | TRP104 | |
1 | TYR8 | |
1 | ARG14 |
site_id | CSA2 |
Number of Residues | 3 |
Details |
Chain | Residue | Details |
2 | TRP104 | |
2 | TYR8 | |
2 | ARG14 |
site_id | MCSA1 |
Number of Residues | 3 |
Details | M-CSA 719 |
Chain | Residue | Details |
1 | TYR8 | electrostatic stabiliser, modifies pKa |
1 | ARG14 | electrostatic stabiliser |
1 | TRP104 | electrostatic stabiliser, steric role |
site_id | MCSA2 |
Number of Residues | 3 |
Details | M-CSA 719 |
Chain | Residue | Details |
2 | TYR8 | electrostatic stabiliser, modifies pKa |
2 | ARG14 | electrostatic stabiliser |
2 | TRP104 | electrostatic stabiliser, steric role |