Structure of PDB 2bx7 Chain A

Receptor sequence
>2bx7A (length=311) Species: 1358 (Lactococcus lactis) [Search protein sequence]
MLNTTFANAKFANPFMNASGVHCMTIEDLEELKASQAGAYITKSSTLEKR
EGNPLPRYVDLELGSINSMGLPNLGFDYYLDYVLKNQKENAQEGPIFFSI
AGMSAAENIAMLKKIQESDFSGITELNLSCPNVPGKPQLAYDFEATEKLL
KEVFTFFTKPLGVKLPPYFDLVHFDIMAEILNQFPLTYVNSVNSIGNGLF
IDPEAESVVIKPKDGFGGIGGAYIKPTALANVRAFYTRLKPEIQIIGTGG
IETGQDAFEHLLCGATMLQIGTALHKEGPAIFDRIIKELEEIMNQKGYQS
IADFHGKLKSL
3D structure
PDB2bx7 Interaction of Benzoate Pyrimidine Analogues with Class 1A Dihydroorotate Dehydrogenase from Lactococcus Lactis.
ChainA
Resolution2.04 Å
3D
structure
Catalytic site residues are labeled in the structure
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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 FMN A A18 S19 G20 K43 S44 N67 M69 N127 K164 V192 N193 G221 T248 G249 G271 T272 A18 S19 G20 K43 S44 N67 M69 N127 K164 V192 N193 G221 T248 G249 G271 T272
BS02 MG A K33 S35 K33 S35
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

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Molecular Function

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Biological Process

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Cellular Component
External links
PDB RCSB:2bx7, PDBe:2bx7, PDBj:2bx7
PDBsum2bx7
PubMed17444658
UniProtA2RJT9|PYRDA_LACLM Dihydroorotate dehydrogenase A (fumarate) (Gene Name=pyrDA)

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