Online Services

●I-TASSER ●I-TASSER-MTD ●C-I-TASSER ●CR-I-TASSER ●QUARK ●C-QUARK ●LOMETS ●MUSTER ●CEthreader ●SEGMER ●DeepFold ●DeepFoldRNA ●FoldDesign ●COFACTOR ●COACH ●MetaGO ●TripletGO ●IonCom ●FG-MD ●ModRefiner ●REMO ●DEMO ●DEMO-EM ●SPRING ●COTH ●Threpp ●PEPPI ●BSpred ●ANGLOR ●EDock ●BSP-SLIM ●SAXSTER ●FUpred ●ThreaDom ●ThreaDomEx ●EvoDesign ●BindProf ●BindProfX ●SSIPe ●GPCR-I-TASSER ●MAGELLAN ●ResQ ●STRUM ●DAMpred

●TM-score ●TM-align ●US-align ●MM-align ●RNA-align ●NW-align ●LS-align ●EDTSurf ●MVP ●MVP-Fit ●SPICKER ●HAAD ●PSSpred ●3DRobot ●MR-REX ●I-TASSER-MR ●SVMSEQ ●NeBcon ●ResPRE ●TripletRes ●DeepPotential ●WDL-RF ●ATPbind ●DockRMSD ●DeepMSA ●FASPR ●EM-Refiner ●GPU-I-TASSER

●BioLiP ●E. coli ●GLASS ●GPCR-HGmod ●GPCR-RD ●GPCR-EXP ●Tara-3D ●TM-fold ●DECOYS ●POTENTIAL ●RW/RWplus ●EvoEF ●HPSF ●THE-DB ●ADDRESS ●Alpaca-Antibody ●CASP7 ●CASP8 ●CASP9 ●CASP10 ●CASP11 ●CASP12 ●CASP13 ●CASP14

Structure of PDB 2cvd Chain C

Receptor sequence >2cvdC (length=198) Species: 9606 (Homo sapiens) [Search protein sequence] PNYKLTYFNMRGRAEIIRYIFAYLDIQYEDHRIEQADWPEIKSTLPFGKI PILEVDGLTLHQSLAIARYLTKNTDLAGNTEMEQCHVDAIVDTLDDFMSC FPWAEKKQDVKEQMFNELLTYNAPHLMQDLDTYLGGREWLIGMSVTWADF YWEICSTTLLVFKPDLLDNHPRLVTLRKKVQAIPAVANWIKRRPQTKL

3D structure PDB 2cvd Structural and Functional Characterization of HQL-79, an Orally Selective Inhibitor of Human Hematopoietic Prostaglandin D Synthase. Chain C Resolution 1.45 Å 3D structure Catalytic site residues are labeled in the structure [Spin on] [Spin off] [Reset orientation] [High quality] [Low quality] [White background] [Black background] [Download] [Download structure with residue number starting from 1]

Enzymatic activity Catalytic site (original residue number in PDB) Y8 R14 R19 W104 Catalytic site (residue number reindexed from 1) Y7 R13 R18 W103 Enzyme Commision number 2.5.1.18: glutathione transferase. 5.3.99.2: prostaglandin-D synthase.

Interaction with ligand Site # Ligand Ligand chain Binding residues on receptor (original residue number in PDB) Binding residues on receptor (residue number reindexed from 1) Binding affinity BS01 GSH C Y8 R14 W39 K43 K50 I51 Q63 S64 Y7 R13 W38 K42 K49 I50 Q62 S63 BS02 HQL C M11 G13 R14 M99 F102 W104 Y152 T159 M10 G12 R13 M98 F101 W103 Y151 T158 MOAD: Kd=0.8uM BindingDB: IC50=3800nM

Gene Ontology Molecular Function GO:0000287 magnesium ion binding GO:0004364 glutathione transferase activity GO:0004667 prostaglandin-D synthase activity GO:0005509 calcium ion binding GO:0005515 protein binding GO:0016740 transferase activity GO:0016853 isomerase activity GO:0042803 protein homodimerization activity GO:0046872 metal ion binding

	Biological Process
GO:0001516	prostaglandin biosynthetic process
GO:0006693	prostaglandin metabolic process
GO:0007165	signal transduction
GO:0007626	locomotory behavior
GO:0009624	response to nematode
GO:0010269	response to selenium ion
GO:2000255	negative regulation of male germ cell proliferation

	Cellular Component
GO:0005654	nucleoplasm
GO:0005737	cytoplasm
GO:0005829	cytosol
GO:0043231	intracellular membrane-bounded organelle

View graph for Molecular Function

View graph for Biological Process

View graph for Cellular Component