Structure of PDB 1uum Chain B Binding Site BS02

Receptor Information
>1uum Chain B (length=350) Species: 10117 (Rattus rattus) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
YAEYLMPGLQRLLDPESAHRLAVRVTSLGLLPRATFQDSDMLEVKVLGHK
FRNPVGIAAGFDKNGEAVDGLYKLGFGFVEVGSVTPQPQEGNPRPRVFRL
PEDQAVINRYGFNSHGLSVVEHRLRARQQKQAQLTADGLPLGINLGKNKT
SEDAAADYAEGVRTLGPLADYLVVNVSSQGKTELRHLLSKVLQERDALKG
TRKPAVLVKIAPDLTAQDKEDIASVARELGIDGLIVTNTTVSRPVGLQGA
LRSETGGLSGKPLRDLSTQTIREMYALTQGRIPIIGVGGVSSGQDALEKI
QAGASLVQLYTALIFLGPPVVVRVKRELEALLKERGFTTVTDAIGADHRR
Ligand information
Ligand IDAFI
InChIInChI=1S/C22H19ClO3/c23-16-11-9-14(10-12-16)13-5-7-15(8-6-13)19-20(24)17-3-1-2-4-18(17)21(25)22(19)26/h1-4,9-13,25-26H,5-8H2/t13-
InChIKeyHKIDMHSZRQSXJE-RNMGOYHCSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.5.0c1ccc2c(c1)C(=C(C(=C3CCC(CC3)c4ccc(cc4)Cl)C2=O)O)O
CACTVS 3.341OC1=C(O)[C](=[C@@]2CC[CH](CC2)c3ccc(Cl)cc3)C(=O)c4ccccc14
CACTVS 3.341OC1=C(O)[C](=[C]2CC[CH](CC2)c3ccc(Cl)cc3)C(=O)c4ccccc14
ACDLabs 10.04O=C3c4ccccc4C(O)=C(O)\C3=C2/CCC(c1ccc(Cl)cc1)CC2
FormulaC22 H19 Cl O3
Name2-[4-(4-CHLOROPHENYL)CYCLOHEXYLIDENE]-3,4-DIHYDROXY-1(2H)-NAPHTHALENONE
ChEMBL
DrugBank
ZINC
PDB chain1uum Chain B Residue 400 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

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PDB1uum Inhibitor Binding in a Class 2 Dihydroorotate Dehydrogenase Causes Variations in the Membrane-Associated N-Terminal Domain
Resolution2.3 Å
Binding residue
(original residue number in PDB)		E40 M43 P44 Q47 P52 A55 H56 V134 R136 Y356 I360 P364
Binding residue
(residue number reindexed from 1)		E3 M6 P7 Q10 P15 A18 H19 V97 R99 Y310 I314 P318
Annotation score1
Binding affinityMOAD: ic50=698nM
Enzymatic activity
Catalytic site (original residue number in PDB) G119 N145 F149 S215 K255 N284
Catalytic site (residue number reindexed from 1) G82 N108 F112 S178 K209 N238
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

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1uum, PDBe:1uum, PDBj:1uum
PDBsum1uum
PubMed15044733
UniProtQ63707|PYRD_RAT Dihydroorotate dehydrogenase (quinone), mitochondrial (Gene Name=Dhodh)

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