Structure of PDB 4oqv Chain A Binding Site BS02

Receptor Information
>4oqv Chain A (length=353) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
DERFYAEHLMPTLQGLLDPESAHRLAVRFTSLGLLPRARFQDSDMLEVRV
LGHKFRNPVGIAAGFDKHGEAVDGLYKMGFGFVEIGSVTPKPQEGNPRPR
VFRLPEDQAVINRYGFNSHGLSVVEHRLRARQQKQAKLTEDGLPLGVNLG
KNKTSVDAAEDYAEGVRVLGPLADYLVVNVSSPGKAELRRLLTKVLQERD
GLRRVHRPAVLVKIAPDLTSQDKEDIASVVKELGIDGLIVTNTTVSRPAG
LQGALRSETGGLSGKPLRDLSTQTIREMYALTQGRVPIIGVGGVSSGQDA
LEKIRAGASLVQLYTALTFWGPPVVGKVKRELEALLKEQGFGGVTDAIGA
DHR
Ligand information
Ligand ID2V6
InChIInChI=1S/C14H7F8N5/c1-5-2-9(27-12(23-5)25-11(26-27)14(20,21)22)24-6-3-7(15)10(8(16)4-6)13(17,18)19/h2-4,24H,1H3
InChIKeyJEEOGRYTTNEULC-UHFFFAOYSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.7.6Cc1cc(n2c(n1)nc(n2)C(F)(F)F)Nc3cc(c(c(c3)F)C(F)(F)F)F
ACDLabs 12.01FC(F)(F)c1c(F)cc(cc1F)Nc2cc(nc3nc(nn23)C(F)(F)F)C
CACTVS 3.385Cc1cc(Nc2cc(F)c(c(F)c2)C(F)(F)F)n3nc(nc3n1)C(F)(F)F
FormulaC14 H7 F8 N5
NameN-[3,5-difluoro-4-(trifluoromethyl)phenyl]-5-methyl-2-(trifluoromethyl)[1,2,4]triazolo[1,5-a]pyrimidin-7-amine
ChEMBLCHEMBL3289672
DrugBank
ZINCZINC000098208311
PDB chain4oqv Chain A Residue 503 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB4oqv Fluorine Modulates Species Selectivity in the Triazolopyrimidine Class of Plasmodium falciparum Dihydroorotate Dehydrogenase Inhibitors.
Resolution1.23 Å
Binding residue
(original residue number in PDB)		M43 L46 Q47 P52 A55 A59 V134 R136 Y356 T360 P364
Binding residue
(residue number reindexed from 1)		M10 L13 Q14 P19 A22 A26 V101 R103 Y314 T318 P322
Annotation score1
Binding affinityMOAD: ic50=1.6uM
BindingDB: IC50=1600nM
Enzymatic activity
Catalytic site (original residue number in PDB) G119 N145 F149 S215 K255 N284
Catalytic site (residue number reindexed from 1) G86 N112 F116 S182 K213 N242
Enzyme Commision number 1.3.5.2: dihydroorotate dehydrogenase (quinone).
Gene Ontology
Molecular Function
GO:0004151 dihydroorotase activity
GO:0004152 dihydroorotate dehydrogenase activity
GO:0005515 protein binding
GO:0016491 oxidoreductase activity
GO:0016627 oxidoreductase activity, acting on the CH-CH group of donors
GO:0106430 dihydroorotate dehydrogenase (quinone) activity
Biological Process
GO:0006207 'de novo' pyrimidine nucleobase biosynthetic process
GO:0006221 pyrimidine nucleotide biosynthetic process
GO:0006225 UDP biosynthetic process
GO:0009220 pyrimidine ribonucleotide biosynthetic process
GO:0044205 'de novo' UMP biosynthetic process
Cellular Component
GO:0005654 nucleoplasm
GO:0005737 cytoplasm
GO:0005739 mitochondrion
GO:0005743 mitochondrial inner membrane
GO:0005829 cytosol
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:4oqv, PDBe:4oqv, PDBj:4oqv
PDBsum4oqv
PubMed24801997
UniProtQ02127|PYRD_HUMAN Dihydroorotate dehydrogenase (quinone), mitochondrial (Gene Name=DHODH)

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