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1PGE

PROSTAGLANDIN H2 SYNTHASE-1 COMPLEXED WITH P-(2'-IODO-5'-THENOYL)HYDROTROPIC ACID (IODOSUPROFEN)

Functional Information from GO Data
ChainGOidnamespacecontents
A0001516biological_processprostaglandin biosynthetic process
A0004601molecular_functionperoxidase activity
A0004666molecular_functionprostaglandin-endoperoxide synthase activity
A0005737cellular_componentcytoplasm
A0005783cellular_componentendoplasmic reticulum
A0005789cellular_componentendoplasmic reticulum membrane
A0006629biological_processlipid metabolic process
A0006631biological_processfatty acid metabolic process
A0006633biological_processfatty acid biosynthetic process
A0006693biological_processprostaglandin metabolic process
A0006979biological_processresponse to oxidative stress
A0008217biological_processregulation of blood pressure
A0016020cellular_componentmembrane
A0016491molecular_functionoxidoreductase activity
A0016702molecular_functionoxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen
A0019371biological_processcyclooxygenase pathway
A0020037molecular_functionheme binding
A0042803molecular_functionprotein homodimerization activity
A0043005cellular_componentneuron projection
A0043231cellular_componentintracellular membrane-bounded organelle
A0046872molecular_functionmetal ion binding
A0051213molecular_functiondioxygenase activity
A0098869biological_processcellular oxidant detoxification
B0001516biological_processprostaglandin biosynthetic process
B0004601molecular_functionperoxidase activity
B0004666molecular_functionprostaglandin-endoperoxide synthase activity
B0005737cellular_componentcytoplasm
B0005783cellular_componentendoplasmic reticulum
B0005789cellular_componentendoplasmic reticulum membrane
B0006629biological_processlipid metabolic process
B0006631biological_processfatty acid metabolic process
B0006633biological_processfatty acid biosynthetic process
B0006693biological_processprostaglandin metabolic process
B0006979biological_processresponse to oxidative stress
B0008217biological_processregulation of blood pressure
B0016020cellular_componentmembrane
B0016491molecular_functionoxidoreductase activity
B0016702molecular_functionoxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen
B0019371biological_processcyclooxygenase pathway
B0020037molecular_functionheme binding
B0042803molecular_functionprotein homodimerization activity
B0043005cellular_componentneuron projection
B0043231cellular_componentintracellular membrane-bounded organelle
B0046872molecular_functionmetal ion binding
B0051213molecular_functiondioxygenase activity
B0098869biological_processcellular oxidant detoxification
Functional Information from PDB Data
site_idCOA
Number of Residues4
DetailsTHE CYCLOOXYGENASE ACTIVE SITE IS LOCATED WITHIN A LONG HYDROPHOBIC CHANNEL AT A REGION DEFINED BY RESIDUES ARG 120, SER 530 (SITE OF ASPIRIN ACETYLATION), TYR 385, AND GLU 524.
ChainResidue
AARG120
ASER530
ATYR385
AGLU524

site_idCOB
Number of Residues4
DetailsTHE CYCLOOXYGENASE ACTIVE SITE IS LOCATED WITHIN A LONG HYDROPHOBIC CHANNEL AT A REGION DEFINED BY RESIDUES ARG 120, SER 530 (SITE OF ASPIRIN ACETYLATION), TYR 385, AND GLU 524.
ChainResidue
BSER530
BTYR385
BGLU524
BARG120

site_idPEA
Number of Residues4
DetailsTHE PEROXIDASE ACTIVE SITE IS AT THE HEME (HEM 601) SITE. HIS 388 IS THE PROXIMAL HEME LIGAND.
ChainResidue
AGLN203
AHIS207
AHIS388
AHEM601

site_idPEB
Number of Residues4
DetailsTHE PEROXIDASE ACTIVE SITE IS AT THE HEME (HEM 601) SITE. HIS 388 IS THE PROXIMAL HEME LIGAND.
ChainResidue
BGLN203
BHIS207
BHIS388
BHEM601

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues72
DetailsTRANSMEM: Helical
ChainResidueDetails
AILE74-LEU82
APRO86-LEU92
AARG97-ALA105
AILE108-ASN122
BILE74-LEU82
BPRO86-LEU92
BARG97-ALA105
BILE108-ASN122

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Proton acceptor
ChainResidueDetails
AHIS207
BHIS207

site_idSWS_FT_FI3
Number of Residues2
DetailsACT_SITE: For cyclooxygenase activity => ECO:0000269|PubMed:2122967
ChainResidueDetails
ATYR385
BTYR385

site_idSWS_FT_FI4
Number of Residues2
DetailsBINDING: axial binding residue
ChainResidueDetails
AHIS388
BHIS388

site_idSWS_FT_FI5
Number of Residues2
DetailsSITE: Not glycosylated => ECO:0000269|PubMed:8349699
ChainResidueDetails
AASN104
BASN104

site_idSWS_FT_FI6
Number of Residues2
DetailsSITE: Aspirin-acetylated serine
ChainResidueDetails
ASER530
BSER530

site_idSWS_FT_FI7
Number of Residues6
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:8349699
ChainResidueDetails
AASN68
AASN144
AASN410
BASN68
BASN144
BASN410

218853

PDB entries from 2024-04-24

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