Structure of PDB 3gye Chain A

Receptor sequence
>3gyeA (length=299) Species: 5664 (Leishmania major) [Search protein sequence]
MSLQVNLLNNTFANPFMNAAGVMCTTTEELVAMTESASGSLVSKSCTPAL
REGNPTPRYQALPLGSINSMGLPNNGFDFYLAYAAEQHDYGKKPLFLSMS
GLSMRENVEMCKRLAAVATEKGVILELNLDFDAMRQCLTAVSEVYPHSFG
VKMPPYFDFAHFDAAAEILNEFPKVQFITCINSIGNGLVIDAETESVVIK
PKQGFGGLGGRYVLPTALANINAFYRRCPGKLIFGCGGVYTGEDAFLHVL
AGASMVQVGTALQEEGPSIFERLTSELLGVMAKKRYQTLDEFRGKVRTL
3D structure
PDB3gye Crystal Structure of Leishmania major Dihydroorotate dehydrogenase
ChainA
Resolution2.0 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 K165 I194
Catalytic site (residue number reindexed from 1) K44 N68 L72 K152 I181
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 FMN A A19 A20 G21 K44 S45 N68 M70 N128 K165 N195 G222 G223 C249 G250 G251 G272 T273 A19 A20 G21 K44 S45 N68 M70 N128 K152 N182 G209 G210 C236 G237 G238 G259 T260
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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Cellular Component
External links
PDB RCSB:3gye, PDBe:3gye, PDBj:3gye
PDBsum3gye
PubMed
UniProtQ4QEW7

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