Structure of PDB 3gz3 Chain A

Receptor sequence

>3gz3A (length=299) Species: 5664 (Leishmania major)

MSLQVNLLNNTFANPFMNAAGVMCTTTEELVAMTESASGSLVSKSCTPAL
REGNPTPRYQALPLGSINSMGLPNNGFDFYLAYAAEQHDYGKKPLFLSMS
GLSMRENVEMCKRLAAVATEKGVILELNLDFDAMRQCLTAVSEVYPHSFG
VKMPPYFDFAHFDAAAEILNEFPKVQFITCINSIGNGLVIDAETESVVIK
PKQGFGGLGGRYVLPTALANINAFYRRCPGKLIFGCGGVYTGEDAFLHVL
AGASMVQVGTALQEEGPSIFERLTSELLGVMAKKRYQTLDEFRGKVRTL

3D structure

• PDB: 3gz3 Leismania major dihydroorotate in complex with orotate
• Chain: A
• Resolution: 1.9 Å

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 Y59 N68 M70 N128 K165 I194 N195 G222 G223 C249 G250 G251 G272 T273	A19 A20 G21 K44 S45 Y59 N68 M70 N128 K152 I181 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

External links

• PDB: RCSB:3gz3, PDBe:3gz3, PDBj:3gz3
• PDBsum: 3gz3
• UniProt: Q4QEW7