Structure of PDB 4cqa Chain B

Receptor sequence
>4cqaB (length=368) Species: 5833 (Plasmodium falciparum) [Search protein sequence]
FFLYDIFLKFCLKYIDGEICHDLFLLLGKYNILPYDTSNDSIYACTNIKH
LDFINPFGVAAGFDKNGVCIDSILKLGFSFIEIGTITPRGQTGNAKPRIF
RDVESRSIINSCGFNNMGCDKVTENLILFRKRQEEDKLLSKHIVGVSIGK
NKDTVNIVDDLKYCINKIGRYADYIAINVSSPNTPGLRDNQEAGKLKNII
LSVKEEIDNLEKNNFLWFNTTKKKPLVFVKLAPDLNQEQKKEIADVLLET
NIDGMIISNTTTQINDIKSFENKKGGVSGAKLKDISTKFICEMYNYTNKQ
IPIIASGGIFSGLDALEKIEAGASVCQLYSCLVFNGMKSAVQIKRELNHL
LYQRGYYNLKEAIGRKHS
3D structure
PDB4cqa In Vitro Resistance Selections for Plasmodium Falciparum Dihydroorotate Dehydrogenase Inhibitors Give Mutants with Multiple Point Mutations in the Drug-Binding Site and Altered Growth.
ChainB
Resolution2.82 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 T348 K429 N458
Catalytic site (residue number reindexed from 1) G84 N110 F114 S181 N183 T184 K230 N259
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 FMN B A225 G226 T249 N274 N342 K429 S477 G478 S505 G506 G507 Y528 S529 A61 G62 T85 N110 N178 K230 S278 G279 S306 G307 G308 Y329 S330
BS02 ID6 B G181 C184 H185 F188 F227 R265 V532 G17 C20 H21 F24 F63 R101 V333 BindingDB: IC50=1.35e+4nM
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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Biological Process
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Cellular Component
External links
PDB RCSB:4cqa, PDBe:4cqa, PDBj:4cqa
PDBsum4cqa
PubMed24782313
UniProtQ08210|PYRD_PLAF7 Dihydroorotate dehydrogenase (quinone), mitochondrial (Gene Name=PFF0160c)

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