Structure of PDB 3fjl Chain A

Receptor sequence

>3fjlA (length=361) Species: 9606 (Homo sapiens) [Search protein sequence]

GDERFYAEHLMPTLQGLLDPESAHRLAVRFTSLGLLPFQDSDMLEVRVLG
HKFRNPVGIAAGFDKHGEAVDGLYKMGFGFVEIGSVTPKPQEGNPRPRVF
RLPEDQAVINRYGFNSHGLSVVEHRLRARQQKQAKLTEDGLPLGVNLGKN
KTSVDAAEDYAEGVRVLGPLADYLVVNVSSPNTAGLRSLQGKAELRRLLT
KVLQERDGLRRVHRPAVLVKIAPDLTSQDKEDIASVVKELGIDGLIVTNT
TVSRPAGLQGALRSETGGLSGKPLRDLSTQTIREMYALTQGRVPIIGVGG
VSSGQDALEKIRAGASLVQLYTALTFWGPPVVGKVKRELEALLKEQGFGG
VTDAIGADHRR

3D structure

PDB

3fjl Structure-based design, synthesis, and characterization of inhibitors of human and Plasmodium falciparum dihydroorotate dehydrogenases

Chain

Resolution

1.9 Å

3D
structure

Catalytic site residues are labeled in the structure
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Enzymatic activity

Catalytic site (original residue number in PDB)	G119 N145 F149 S215 N217 T218 K255 N284
Catalytic site (residue number reindexed from 1)	G84 N110 F114 S180 N182 T183 K220 N249
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	A	A96 G97 K100 S120 N145 N181 N212 K255 N284 T285 S305 G306 V333 G334 G335 L355 Y356 T357	A61 G62 K65 S85 N110 N146 N177 K220 N249 T250 S270 G271 V298 G299 G300 L320 Y321 T322
BS02	CJH	A	M43 L46 P52 H56 A59 F62 L68 R136 Y356 T360 P364	M11 L14 P20 H24 A27 F30 L36 R101 Y321 T325 P329	MOAD: ic50=0.13uM

Gene Ontology

	Molecular Function
GO:0004151	dihydroorotase activity
GO:0004152	dihydroorotate dehydrogenase activity
GO:0005515	protein binding
GO:0016491	oxidoreductase activity
GO:0016627	oxidoreductase activity, acting on the CH-CH group of donors
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:0009220	pyrimidine ribonucleotide biosynthetic process
GO:0044205	'de novo' UMP biosynthetic process

	Cellular Component
GO:0005654	nucleoplasm
GO:0005737	cytoplasm
GO:0005739	mitochondrion
GO:0005743	mitochondrial inner membrane
GO:0005829	cytosol
GO:0016020	membrane

View graph for
Molecular Function

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Biological Process

View graph for
Cellular Component

External links

PDB	RCSB:3fjl, PDBe:3fjl, PDBj:3fjl
PDBsum	3fjl
PubMed	19351152
UniProt	Q02127\|PYRD_HUMAN Dihydroorotate dehydrogenase (quinone), mitochondrial (Gene Name=DHODH)

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