1FE2
CRYSTAL STRUCTURE OF DIHOMO-GAMMA-LINOLEIC 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 | 0006629 | biological_process | lipid metabolic process |
A | 0006631 | biological_process | fatty acid metabolic process |
A | 0006633 | biological_process | fatty acid biosynthetic process |
A | 0006693 | biological_process | prostaglandin metabolic process |
A | 0006979 | biological_process | response to oxidative stress |
A | 0008217 | biological_process | regulation of blood pressure |
A | 0016020 | cellular_component | membrane |
A | 0016491 | molecular_function | oxidoreductase activity |
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 | 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 | Transmembrane: {"description":"Helical"} |
Chain | Residue | Details |
site_id | SWS_FT_FI2 |
Number of Residues | 38 |
Details | Domain: {"description":"EGF-like","evidences":[{"source":"PROSITE-ProRule","id":"PRU00076","evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI3 |
Number of Residues | 1 |
Details | Active site: {"description":"Proton acceptor"} |
Chain | Residue | Details |
site_id | SWS_FT_FI4 |
Number of Residues | 1 |
Details | Active site: {"description":"For cyclooxygenase activity","evidences":[{"source":"PubMed","id":"2122967","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI5 |
Number of Residues | 1 |
Details | Binding site: {"description":"axial binding residue"} |
Chain | Residue | Details |
site_id | SWS_FT_FI6 |
Number of Residues | 1 |
Details | Site: {"description":"Not glycosylated","evidences":[{"source":"PubMed","id":"8349699","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI7 |
Number of Residues | 1 |
Details | Site: {"description":"Aspirin-acetylated serine"} |
Chain | Residue | Details |
site_id | SWS_FT_FI8 |
Number of Residues | 3 |
Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"8349699","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
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 |