Structure of PDB 1jue Chain A

Receptor sequence

>1jueA (length=311) Species: 1358 (Lactococcus lactis)

MLNTTFANAKFANPFMNASGVHCMTIEDLEELKASQAGAYITKSSTLEKR
EGNPLPRYVDLELGSINSMGLPNLGFDYYLDYVLKNQKENAQEGPIFFSI
AGMSAAENIAMLKKIQESDFSGITELNLSCPNVPGKPQLAYDFEATEKLL
KEVFTFFTKPLGVKLPPYFDLVHFDIMAEILNQFPLTYVNSVNSIGNGLF
IDPEAESVVIKPKDGFGGIGGAYIKPTALANVRAFYTRLKPEIQIIGTGG
IETGQDAFEHLLCGATMLQIGTALHKEGPAIFDRIIKELEEIMNQKGYQS
IADFHGKLKSL

3D structure

• PDB: 1jue Lactococcus lactis dihydroorotate dehydrogenase A mutants reveal important facets of the enzymatic function
• Chain: A
• Resolution: 1.8 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): K43 N67 L71 C130 N132 V133 K164 V192
• Catalytic site (residue number reindexed from 1): K43 N67 L71 C130 N132 V133 K164 V192
• 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	MG	A	K33 S35	K33 S35
BS02	FMN	A	A18 S19 G20 K43 S44 N67 M69 N127 K164 N193 G221 I224 T248 G249 G250 G271 T272	A18 S19 G20 K43 S44 N67 M69 N127 K164 N193 G221 I224 T248 G249 G250 G271 T272

Gene Ontology

Molecular Function

• 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: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:0005737 cytoplasm

External links

• PDB: RCSB:1jue, PDBe:1jue, PDBj:1jue
• PDBsum: 1jue
• PubMed: 12732650
• UniProt: A2RJT9|PYRDA_LACLM Dihydroorotate dehydrogenase A (fumarate) (Gene Name=pyrDA)