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2IAG

Crystal structure of human prostacyclin synthase

Functional Information from GO Data
ChainGOidnamespacecontents
A0001516biological_processprostaglandin biosynthetic process
A0004497molecular_functionmonooxygenase activity
A0005506molecular_functioniron ion binding
A0005515molecular_functionprotein binding
A0005615cellular_componentextracellular space
A0005634cellular_componentnucleus
A0005783cellular_componentendoplasmic reticulum
A0005789cellular_componentendoplasmic reticulum membrane
A0005901cellular_componentcaveola
A0006629biological_processlipid metabolic process
A0006690biological_processicosanoid metabolic process
A0008116molecular_functionprostaglandin-I synthase activity
A0016020cellular_componentmembrane
A0016705molecular_functionoxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
A0016829molecular_functionlyase activity
A0016853molecular_functionisomerase activity
A0019371biological_processcyclooxygenase pathway
A0020037molecular_functionheme binding
A0032088biological_processnegative regulation of NF-kappaB transcription factor activity
A0034356biological_processNAD biosynthesis via nicotinamide riboside salvage pathway
A0035360biological_processpositive regulation of peroxisome proliferator activated receptor signaling pathway
A0045019biological_processnegative regulation of nitric oxide biosynthetic process
A0045766biological_processpositive regulation of angiogenesis
A0046872molecular_functionmetal ion binding
A0050728biological_processnegative regulation of inflammatory response
A0071347biological_processcellular response to interleukin-1
A0071354biological_processcellular response to interleukin-6
A0071456biological_processcellular response to hypoxia
A0097190biological_processapoptotic signaling pathway
A0106256molecular_functionhydroperoxy icosatetraenoate dehydratase activity
A1900119biological_processpositive regulation of execution phase of apoptosis
B0001516biological_processprostaglandin biosynthetic process
B0004497molecular_functionmonooxygenase activity
B0005506molecular_functioniron ion binding
B0005515molecular_functionprotein binding
B0005615cellular_componentextracellular space
B0005634cellular_componentnucleus
B0005783cellular_componentendoplasmic reticulum
B0005789cellular_componentendoplasmic reticulum membrane
B0005901cellular_componentcaveola
B0006629biological_processlipid metabolic process
B0006690biological_processicosanoid metabolic process
B0008116molecular_functionprostaglandin-I synthase activity
B0016020cellular_componentmembrane
B0016705molecular_functionoxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
B0016829molecular_functionlyase activity
B0016853molecular_functionisomerase activity
B0019371biological_processcyclooxygenase pathway
B0020037molecular_functionheme binding
B0032088biological_processnegative regulation of NF-kappaB transcription factor activity
B0034356biological_processNAD biosynthesis via nicotinamide riboside salvage pathway
B0035360biological_processpositive regulation of peroxisome proliferator activated receptor signaling pathway
B0045019biological_processnegative regulation of nitric oxide biosynthetic process
B0045766biological_processpositive regulation of angiogenesis
B0046872molecular_functionmetal ion binding
B0050728biological_processnegative regulation of inflammatory response
B0071347biological_processcellular response to interleukin-1
B0071354biological_processcellular response to interleukin-6
B0071456biological_processcellular response to hypoxia
B0097190biological_processapoptotic signaling pathway
B0106256molecular_functionhydroperoxy icosatetraenoate dehydratase activity
B1900119biological_processpositive regulation of execution phase of apoptosis
Functional Information from PDB Data
site_idAC1
Number of Residues17
DetailsBINDING SITE FOR RESIDUE HEM A 600
ChainResidue
AMET124
ACYS441
ALEU442
AGLY443
ATYR446
AALA447
ALEU485
AHOH807
AHOH812
AGLN280
AALA283
ATHR284
AASN287
APRO433
ATRP434
AGLY435
AASN439

site_idAC2
Number of Residues19
DetailsBINDING SITE FOR RESIDUE HEM B 600
ChainResidue
BLYS121
BMET124
BLEU128
BALA283
BTHR284
BASN287
BMET288
BPRO355
BPRO433
BTRP434
BGLY435
BASN439
BCYS441
BLEU442
BGLY443
BALA447
BLEU485
BHOH919
BHOH921

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues10
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:F1RE08
ChainResidueDetails
AARG106
BARG382
ALEU112
AASN287
ATHR358
AARG382
BARG106
BLEU112
BASN287
BTHR358

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: axial binding residue => ECO:0000269|PubMed:17020766, ECO:0000269|PubMed:18032380, ECO:0007744|PDB:2IAG, ECO:0007744|PDB:3B6H
ChainResidueDetails
ACYS441
BCYS441

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PDB entries from 2024-07-24

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