Structure of PDB 3b6h Chain A Binding Site BS01

Receptor Information
>3b6h Chain A (length=469) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
RTRRPGEPPLDLGSIPWLGYALDFGKDAASFLTRMKEKHGDIFTILVGGR
YVTVLLDPHSYDAVVWEPRTRLDFHAYAIFLMERIFDVQLPHYSPSDEKA
RMKLTLLHRELQALTEAMYTNLHAVLLGDATEAGSGWHEMGLLDFSYSFL
LRAGYLTLYGIEALPRTHESQAQDRVHSADVFHTFRQLDRLLPKLARGSL
SVGDKDHMCSVKSRLWKLLSPARLARRAHRSKWLESYLLHLEEMGVSEEM
QARALVLQLWATQGNMGPAAFWLLLFLLKNPEALAAVRGELESILWQLPQ
KVLDSTPVLDSVLSESLRLTAAPFITREVVVDLAMPMADGREFNLRRGDR
LLLFPFLSPQRDPEIYTDPEVFKYNRFLNPDGSEKKDFYKDGKRLKNYNM
PWGAGHNHCLGRSYAVNSIKQFVFLVLVHLDLELINADVEIPEFDLSRYG
FGLMQPEHDVPVRYRIRPH
Ligand information
Ligand IDMXD
InChIInChI=1S/C9H15N5O/c10-7-6-8(12-9(11)14(7)15)13-4-2-1-3-5-13/h6H,1-5,10H2,(H2,11,12)
InChIKeyZFMITUMMTDLWHR-UHFFFAOYSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.5.0c1c([n+](c(nc1N2CCCCC2)N)[O-])N
CACTVS 3.341Nc1cc(nc(N)[n+]1[O-])N2CCCCC2
ACDLabs 10.04[O-][n+]1c(nc(cc1N)N2CCCCC2)N
FormulaC9 H15 N5 O
Name6-PIPERIDIN-1-YLPYRIMIDINE-2,4-DIAMINE 3-OXIDE;
MINOXIDIL
ChEMBLCHEMBL802
DrugBankDB00350
ZINCZINC000000001735
PDB chain3b6h Chain A Residue 551 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB3b6h Structures of Prostacyclin Synthase and Its Complexes with Substrate Analog and Inhibitor Reveal a Ligand-specific Heme Conformation Change
Resolution1.62 Å
Binding residue
(original residue number in PDB)		Y99 A100 A283
Binding residue
(residue number reindexed from 1)		Y77 A78 A261
Annotation score1
Binding affinityMOAD: Kd=3.4uM
Enzymatic activity
Enzyme Commision number 4.2.1.152: hydroperoxy icosatetraenoate dehydratase.
5.3.99.4: prostaglandin-I synthase.
Gene Ontology
Molecular Function
GO:0004497 monooxygenase activity
GO:0005506 iron ion binding
GO:0005515 protein binding
GO:0008116 prostaglandin-I synthase activity
GO:0016705 oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
GO:0016829 lyase activity
GO:0016853 isomerase activity
GO:0020037 heme binding
GO:0046872 metal ion binding
GO:0106256 hydroperoxy icosatetraenoate dehydratase activity
Biological Process
GO:0001516 prostaglandin biosynthetic process
GO:0006629 lipid metabolic process
GO:0006690 icosanoid metabolic process
GO:0019371 cyclooxygenase pathway
GO:0032088 negative regulation of NF-kappaB transcription factor activity
GO:0034356 NAD biosynthesis via nicotinamide riboside salvage pathway
GO:0035360 positive regulation of peroxisome proliferator activated receptor signaling pathway
GO:0045019 negative regulation of nitric oxide biosynthetic process
GO:0045766 positive regulation of angiogenesis
GO:0050728 negative regulation of inflammatory response
GO:0071347 cellular response to interleukin-1
GO:0071354 cellular response to interleukin-6
GO:0071456 cellular response to hypoxia
GO:0097190 apoptotic signaling pathway
GO:1900119 positive regulation of execution phase of apoptosis
Cellular Component
GO:0005615 extracellular space
GO:0005634 nucleus
GO:0005783 endoplasmic reticulum
GO:0005789 endoplasmic reticulum membrane
GO:0005901 caveola
GO:0016020 membrane

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:3b6h, PDBe:3b6h, PDBj:3b6h
PDBsum3b6h
PubMed18032380
UniProtQ16647|PTGIS_HUMAN Prostacyclin synthase (Gene Name=PTGIS)

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