1IGX
Crystal Structure of Eicosapentanoic Acid Bound in the Cyclooxygenase Channel of Prostaglandin Endoperoxide H Synthase-1.
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0001516 | biological_process | prostaglandin biosynthetic process |
| A | 0004601 | molecular_function | peroxidase activity |
| A | 0004666 | molecular_function | prostaglandin-endoperoxide synthase activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005783 | cellular_component | endoplasmic reticulum |
| A | 0005789 | cellular_component | endoplasmic reticulum membrane |
| A | 0006979 | biological_process | response to oxidative stress |
| A | 0008217 | biological_process | regulation of blood pressure |
| A | 0016020 | cellular_component | membrane |
| A | 0016702 | molecular_function | oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen |
| A | 0019371 | biological_process | cyclooxygenase pathway |
| A | 0020037 | molecular_function | heme binding |
| A | 0042803 | molecular_function | protein homodimerization activity |
| A | 0043005 | cellular_component | neuron projection |
| A | 0043231 | cellular_component | intracellular membrane-bounded organelle |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0051213 | molecular_function | dioxygenase activity |
| A | 0098869 | biological_process | cellular oxidant detoxification |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 36 |
| Details | TRANSMEM: Helical |
| Chain | Residue | Details |
| A | ILE74-LEU82 | |
| A | PRO86-LEU92 | |
| A | ARG97-ALA105 | |
| A | ILE108-ASN122 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | ACT_SITE: Proton acceptor |
| Chain | Residue | Details |
| A | HIS207 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | ACT_SITE: For cyclooxygenase activity => ECO:0000269|PubMed:2122967 |
| Chain | Residue | Details |
| A | TYR385 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | BINDING: axial binding residue |
| Chain | Residue | Details |
| A | HIS388 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | SITE: Not glycosylated => ECO:0000269|PubMed:8349699 |
| Chain | Residue | Details |
| A | ASN104 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | SITE: Aspirin-acetylated serine |
| Chain | Residue | Details |
| A | SER530 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 3 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:8349699 |
| Chain | Residue | Details |
| A | ASN68 | |
| A | ASN144 | |
| A | ASN410 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1mhl |
| Chain | Residue | Details |
| A | VAL291 |
| site_id | CSA2 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1mhl |
| Chain | Residue | Details |
| A | HIS207 | |
| A | TYR385 | |
| A | GLN203 |
