Structure of PDB 4ef9 Chain A

Receptor sequence
>4ef9A (length=313) Species: 5664 (Leishmania major) [Search protein sequence]
SMSLQVNLLNNTFANPFMNAAGVMCTTTEELVAMTESASGSLVSKSCTPA
LREGNPTPRYQALPLGSINSMGLPNNGFDFYLAYAAEQHDYGKKPLFLSM
SGLSMRENVEMCKRLAAVATEKGVILELNLSCPNVPGKPQVAYDFDAMRQ
CLTAVSEVYPHSFGVKMPPYFDFAHFDAAAEILNEFPKVQFITCINSIGN
GLVIDAETESVVIKPKQGFGGLGGRYVLPTALANINAFYRRCPGKLIFGC
GGVYTGEDAFLHVLAGASMVQVGTALQEEGPSIFERLTSELLGVMAKKRY
QTLDEFRGKVRTL
3D structure
PDB4ef9 Target sites for the design of anti-trypanosomatid drugs based on the structure of dihydroorotate dehydrogenase.
ChainA
Resolution1.6 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) K44 N68 L72 C131 N133 V134 K165 I194
Catalytic site (residue number reindexed from 1) K45 N69 L73 C132 N134 V135 K166 I195
Enzyme Commision number 1.3.98.1: dihydroorotate oxidase (fumarate).
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 4NF A G101 L102 S103 M104 N107 V140 C150 G102 L103 S104 M105 N108 V141 C151
BS02 FMN A A19 A20 G21 K44 S45 Y59 N68 M70 N128 K165 N195 G223 C249 G250 G251 G272 T273 A20 A21 G22 K45 S46 Y60 N69 M71 N129 K166 N196 G224 C250 G251 G252 G273 T274
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0004152 dihydroorotate dehydrogenase activity
GO:0016491 oxidoreductase activity
GO:0016627 oxidoreductase activity, acting on the CH-CH group of donors
GO:1990663 dihydroorotate dehydrogenase (fumarate) activity
Biological Process
GO:0006106 fumarate metabolic process
GO:0006207 'de novo' pyrimidine nucleobase biosynthetic process
GO:0006221 pyrimidine nucleotide biosynthetic process
GO:0006222 UMP biosynthetic process
GO:0044205 'de novo' UMP biosynthetic process
Cellular Component
GO:0005654 nucleoplasm
GO:0005737 cytoplasm
GO:0097014 ciliary plasm

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:4ef9, PDBe:4ef9, PDBj:4ef9
PDBsum4ef9
PubMed23116399
UniProtQ4QEW7

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