Structure of PDB 3i65 Chain A

Receptor sequence
>3i65A (length=370) Species: 36329 (Plasmodium falciparum 3D7) [Search protein sequence]
SYNPEFFLYDIFLKFCLKYIDGEICHDLFLLLGKYNILPYDTSNDSIYAC
TNIKHLDFINPFGVAAGFDKNGVCIDSILKLGFSFIEIGTITPRGQTGNA
KPRIFRDVESRSIINSCGFNNMGCDKVTENLILFRKRQEEDKLLSKHIVG
VSIGKNKDTVNIVDDLKYCINKIGRYADYIAINVSSPNEAGKLKNIILSV
KEEIDNLEKNNIMNDEFLWFNTTKKKPLVFVKLAPDLNQEQKKEIADVLL
ETNIDGMIISNTTTQINDIKSFENKKGGVSGAKLKDISTKFICEMYNYTN
KQIPIIASGGIFSGLDALEKIEAGASVCQLYSCLVFNGMKSAVQIKRELN
HLLYQRGYYNLKEAIGRKHS
3D structure
PDB3i65 Structural plasticity of malaria dihydroorotate dehydrogenase allows selective binding of diverse chemical scaffolds.
ChainA
Resolution2.0 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) G248 N274 F278 S345 N347 K429 N458
Catalytic site (residue number reindexed from 1) G89 N115 F119 S186 N188 K232 N261
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 JZ8 A G181 C184 H185 F188 L189 F227 R265 L531 V532 M536 G22 C25 H26 F29 L30 F68 R106 L334 V335 M339 MOAD: ic50=0.047uM
BS02 FMN A A225 G226 K229 T249 I263 N274 N342 K429 S477 G478 S505 G506 G507 Y528 S529 A66 G67 K70 T90 I104 N115 N183 K232 S280 G281 S308 G309 G310 Y331 S332
Gene Ontology
Molecular Function
GO:0004152 dihydroorotate dehydrogenase activity
GO:0016627 oxidoreductase activity, acting on the CH-CH group of donors
Biological Process
GO:0006207 'de novo' pyrimidine nucleobase biosynthetic process
Cellular Component
GO:0005737 cytoplasm
GO:0016020 membrane

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Molecular Function
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Cellular Component
External links
PDB RCSB:3i65, PDBe:3i65, PDBj:3i65
PDBsum3i65
PubMed19640844
UniProtQ08210|PYRD_PLAF7 Dihydroorotate dehydrogenase (quinone), mitochondrial (Gene Name=PFF0160c)

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