Structure of PDB 6vty Chain D

Receptor sequence
>6vtyD (length=368) Species: 36329 (Plasmodium falciparum 3D7) [Search protein sequence]
PEFFLYDIFLKFCLKYIDGEICHDLFLLLGKYNILPYDTSNDSIYACTNI
KHLDFINPFGVAAGFDKNGVCIDSILKLGFSFIEIGTITPRGQTGNAKPR
IFRDVESRSIINSCGFNNMGCDKVTENLILFRKRQEEDKLLSKHIVGVSI
GKNKDTVNIVDDLKYCINKIGRYADYIAINVSSPNTPGLRDNQEAGKLKN
IILSVKEEIDNLEKNFLWFNTTKKKPLVFVKLAPDLNQEQKKEIADVLLE
TNIDGMIISNTTTQINDIKSFENKKGGVSGAKLKDISTKFICEMYNYTNK
QIPIIASGGIFSGLDALEKIEAGASVCQLYSCLVFNGMKSAVQIKRELNH
LLYQRGYYNLKEAIGRKH
3D structure
PDB6vty Lead Optimization of a Pyrrole-Based Dihydroorotate Dehydrogenase Inhibitor Series for the Treatment of Malaria.
ChainD
Resolution1.78 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) N274 F278 S345 N347 T348 K429 N458
Catalytic site (residue number reindexed from 1) N112 F116 S183 N185 T186 K231 N260
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 RLA D L172 G181 C184 H185 L187 F188 F227 I263 R265 V532 M536 L10 G19 C22 H23 L25 F26 F65 I101 R103 V334 M338 MOAD: ic50=0.1uM
BS02 FMN D A225 G226 T249 N274 N342 K429 S477 G478 S505 G506 G507 Y528 S529 A63 G64 T87 N112 N180 K231 S279 G280 S307 G308 G309 Y330 S331
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:6vty, PDBe:6vty, PDBj:6vty
PDBsum6vty
PubMed32248693
UniProtQ08210|PYRD_PLAF7 Dihydroorotate dehydrogenase (quinone), mitochondrial (Gene Name=PFF0160c)

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