Structure of PDB 4ori Chain A Binding Site BS02

Receptor Information
>4ori Chain A (length=355) Species: 10116 (Rattus norvegicus) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
HFYAEYLMPGLQRLLDPESAHRLAVRVTSLGLLPRATFQDSDMLEVKVLG
HKFRNPVGIAAGFDKNGEAVDGLYKLGFGFVEVGSVTPQPQEGNPRPRVF
RLPEDQAVINRYGFNSHGLSVVEHRLRARQQKQAQLTADGLPLGINLGKN
KTSEDAAADYAEGVRTLGPLADYLVVNVSSPNTQGKTELRHLLSKVLQER
DALKGTRKPAVLVKIAPDLTAQDKEDIASVARELGIDGLIVTNTTVSRPV
GLQGALRSETGGLSGKPLRDLSTQTIREMYALTQGRIPIIGVGGVSSGQD
ALEKIQAGASLVQLYTALIFLGPPVVVRVKRELEALLKERGFTTVTDAIG
ADHRR
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 chain4ori Chain A Residue 502 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
PDB4ori Fluorine Modulates Species Selectivity in the Triazolopyrimidine Class of Plasmodium falciparum Dihydroorotate Dehydrogenase Inhibitors.
Resolution1.5 Å
Binding residue
(original residue number in PDB)		M43 L46 Q47 P52 A55 A59 V134 R136 I360 P364
Binding residue
(residue number reindexed from 1)		M8 L11 Q12 P17 A20 A24 V99 R101 I319 P323
Annotation score1
Binding affinityMOAD: ic50=0.088uM
BindingDB: IC50=49nM
Enzymatic activity
Catalytic site (original residue number in PDB) G119 N145 F149 S215 N217 T218 K255 N284
Catalytic site (residue number reindexed from 1) G84 N110 F114 S180 N182 T183 K214 N243
Enzyme Commision number 1.3.5.2: dihydroorotate dehydrogenase (quinone).
Gene Ontology
Molecular Function
GO:0004151 dihydroorotase activity
GO:0004152 dihydroorotate dehydrogenase activity
GO:0010181 FMN binding
GO:0016491 oxidoreductase activity
GO:0016627 oxidoreductase activity, acting on the CH-CH group of donors
GO:0048038 quinone binding
GO:0048039 ubiquinone binding
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:0007565 female pregnancy
GO:0007595 lactation
GO:0009220 pyrimidine ribonucleotide biosynthetic process
GO:0009410 response to xenobiotic stimulus
GO:0014070 response to organic cyclic compound
GO:0031000 response to caffeine
GO:0042594 response to starvation
GO:0043065 positive regulation of apoptotic process
GO:0044205 'de novo' UMP biosynthetic process
GO:0090140 regulation of mitochondrial fission
GO:1903576 response to L-arginine
Cellular Component
GO:0005737 cytoplasm
GO:0005739 mitochondrion
GO:0005743 mitochondrial inner membrane
GO:0016020 membrane
GO:0043025 neuronal cell body

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:4ori, PDBe:4ori, PDBj:4ori
PDBsum4ori
PubMed24801997
UniProtQ63707|PYRD_RAT Dihydroorotate dehydrogenase (quinone), mitochondrial (Gene Name=Dhodh)

[Back to BioLiP]