Structure of PDB 1uuo Chain A

Receptor sequence
>1uuoA (length=351) Species: 10117 (Rattus rattus) [Search protein sequence]
DDHFYAEYLMPGLQRLLDPESAHRLAVRVTSLGLLPQDSDMLEVKVLGHK
FRNPVGIAAGFDKNGEAVDGLYKLGFGFVEVGSVTPQPQEGNPRPRVFRL
PEDQAVINRYGFNSHGLSVVEHRLRARQQKQAQLTADGLPLGINLGKNKT
SEDAAADYAEGVRTLGPLADYLVVNVSSPQGKTELRHLLSKVLQERDALK
GTRKPAVLVKIAPDLTAQDKEDIASVARELGIDGLIVTNTTVSRPVGLQG
ALRSETGGLSGKPLRDLSTQTIREMYALTQGRIPIIGVGGVSSGQDALEK
IQAGASLVQLYTALIFLGPPVVVRVKRELEALLKERGFTTVTDAIGADHR
R
3D structure
PDB1uuo Inhibitor Binding in a Class 2 Dihydroorotate Dehydrogenase Causes Variations in the Membrane-Associated N-Terminal Domain
ChainA
Resolution2.44 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) G119 N145 F149 S215 K255 N284
Catalytic site (residue number reindexed from 1) G82 N108 F112 S178 K210 N239
Enzyme Commision number 1.3.5.2: dihydroorotate dehydrogenase (quinone).
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 BRF A M43 L46 P52 A55 H56 A59 R136 I360 P364 M10 L13 P19 A22 H23 A26 R99 I315 P319 MOAD: ic50=6nM
BindingDB: IC50=367nM
BS02 FMN A A96 G97 K100 G119 S120 N145 N181 N212 K255 N284 S305 G306 V333 G334 G335 Y356 T357 A59 G60 K63 G82 S83 N108 N144 N175 K210 N239 S260 G261 V288 G289 G290 Y311 T312
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:1uuo, PDBe:1uuo, PDBj:1uuo
PDBsum1uuo
PubMed15044733
UniProtQ63707|PYRD_RAT Dihydroorotate dehydrogenase (quinone), mitochondrial (Gene Name=Dhodh)

[Back to BioLiP]