1PRH
THE X-RAY CRYSTAL STRUCTURE OF THE MEMBRANE PROTEIN PROSTAGLANDIN H2 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 |
| B | 0001516 | biological_process | prostaglandin biosynthetic process |
| B | 0004601 | molecular_function | peroxidase activity |
| B | 0004666 | molecular_function | prostaglandin-endoperoxide synthase activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005783 | cellular_component | endoplasmic reticulum |
| B | 0005789 | cellular_component | endoplasmic reticulum membrane |
| B | 0006629 | biological_process | lipid metabolic process |
| B | 0006631 | biological_process | fatty acid metabolic process |
| B | 0006633 | biological_process | fatty acid biosynthetic process |
| B | 0006693 | biological_process | prostaglandin metabolic process |
| B | 0006979 | biological_process | response to oxidative stress |
| B | 0008217 | biological_process | regulation of blood pressure |
| B | 0016020 | cellular_component | membrane |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0016702 | molecular_function | oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen |
| B | 0019371 | biological_process | cyclooxygenase pathway |
| B | 0020037 | molecular_function | heme binding |
| B | 0042803 | molecular_function | protein homodimerization activity |
| B | 0043005 | cellular_component | neuron projection |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0051213 | molecular_function | dioxygenase activity |
| B | 0098869 | biological_process | cellular oxidant detoxification |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE HEM A 601 |
| Chain | Residue |
| A | ALA199 |
| A | GLN203 |
| A | THR206 |
| A | HIS207 |
| A | PHE210 |
| A | THR212 |
| A | LEU295 |
| A | ASN382 |
| A | TYR385 |
| A | HIS386 |
| A | HIS388 |
| A | LEU390 |
| A | MET391 |
| A | LEU408 |
| A | ILE444 |
| A | ASP450 |
| A | TYR148 |
| site_id | AC2 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE HEM B 601 |
| Chain | Residue |
| B | TYR148 |
| B | ALA199 |
| B | GLN203 |
| B | THR206 |
| B | HIS207 |
| B | PHE210 |
| B | THR212 |
| B | LEU295 |
| B | ASN382 |
| B | TYR385 |
| B | HIS386 |
| B | HIS388 |
| B | LEU390 |
| B | MET391 |
| B | LEU408 |
| B | ILE444 |
| B | ASP450 |
| site_id | COX |
| Number of Residues | 4 |
| Details | CYCLOOXYGENASE ACTIVE SITE IS LOCATED WITHIN A LONG HYDROPHOBIC CHANNEL |
| Chain | Residue |
| A | ARG120 |
| A | SER530 |
| A | TYR385 |
| A | GLU524 |
| site_id | PER |
| Number of Residues | 4 |
| Details | PEROXIDASE ACTIVE SITE IS AT THE HEME (HEM 601) SITE |
| Chain | Residue |
| A | GLN203 |
| A | HIS207 |
| A | HIS388 |
| A | HEM601 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 72 |
| Details | Transmembrane: {"description":"Helical"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton acceptor"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Active site: {"description":"For cyclooxygenase activity","evidences":[{"source":"PubMed","id":"2122967","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Binding site: {"description":"axial binding residue"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | Site: {"description":"Not glycosylated","evidences":[{"source":"PubMed","id":"8349699","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | Site: {"description":"Aspirin-acetylated serine"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 6 |
| 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 | 1 |
| Details | Annotated By Reference To The Literature 1mhl |
| Chain | Residue | Details |
| B | VAL291 |
| site_id | CSA3 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1mhl |
| Chain | Residue | Details |
| A | HIS207 | |
| A | TYR385 | |
| A | GLN203 |
| site_id | CSA4 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1mhl |
| Chain | Residue | Details |
| B | HIS207 | |
| B | TYR385 | |
| B | GLN203 |
