Structure of PDB 2prl Chain A

Receptor sequence

>2prlA (length=367) Species: 9606 (Homo sapiens) [Search protein sequence]

MATGDERFYAEHLMPTLQGLLDPESAHRLAVRFTSLGLLPRARFQDSDML
EVRVLGHKFRNPVGIAAGFDKHGEAVDGLYKMGFGFVEIGSVTPKPQEGN
PRPRVFRLPEDQAVINRYGFNSHGLSVVEHRLRARQQKQAKLTEDGLPLG
VNLGKNKTSVDAAEDYAEGVRVLGPLADYLVVNVSSPNTAGLRSLQGKAE
LRRLLTKVLQERDGLRRVHRPAVLVKIAPDLTSQDKEDIASVVKELGIDG
LIVTNTTVSRPAGLQGALRSETGGLSGKPLRDLSTQTIREMYALTQGRVP
IIGVGGVSSGQDALEKIRAGASLVQLYTALTFWGPPVVGKVKRELEALLK
EQGFGGVTDAIGADHRR

3D structure

PDB

2prl The structures of human dihydroorotate dehydrogenase with and without inhibitor reveal conformational flexibility in the inhibitor and substrate binding sites

Chain

Resolution

2.1 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)	G90 N116 F120 S186 N188 T189 K226 N255
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 Y147 N181 N212 K255 N284 T285 S305 G306 V333 G334 G335 L355 Y356 T357	A67 G68 K71 S91 N116 Y118 N152 N183 K226 N255 T256 S276 G277 V304 G305 G306 L326 Y327 T328
BS02	R2C	A	Y38 M43 L46 Q47 P52 A55 H56 A59 R136 Y356 T360 P364	Y9 M14 L17 Q18 P23 A26 H27 A30 R107 Y327 T331 P335	MOAD: ic50=81nM

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

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Molecular Function

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Biological Process

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Cellular Component

External links

PDB	RCSB:2prl, PDBe:2prl, PDBj:2prl
PDBsum	2prl
PubMed	18672895
UniProt	Q02127\|PYRD_HUMAN Dihydroorotate dehydrogenase (quinone), mitochondrial (Gene Name=DHODH)

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