Structure of PDB 3oix Chain B

Receptor sequence
>3oixB (length=310) Species: 1309 (Streptococcus mutans) [Search protein sequence]
VSTHTTIGSFDFDNCLMNAAGVYCMTREELAAIDHSEAGSFVTKTGTLEE
RAGNPQPRYADTKLGSINSMGLPNLGINYYLDYVTELQKQPDSKNHFLSL
VGMSPEETHTILKMVEASKYQGLVELNLSCPNVPGKPQIAYDFETTDQIL
SEVFTYFTKPLGIKLPPYFDIVHFDQAAAIFNKYPLTFVNCINSIGNGLV
IEDETVVIKPKNGFGGIGGDYVKPTALANVHAFYKRLNPSIQIIGTGGVK
TGRDAFEHILCGASMVQIGTALHQEGPQIFKRITKELKAIMTEKGYETLE
DFRGKLNAMA
3D structure
PDB3oix Structure of the putative dihydroorotate dehydrogenase from Streptococcus mutans
ChainB
Resolution2.399 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) K45 N69 L73 C131 N133 V134 K165 I193
Catalytic site (residue number reindexed from 1) K44 N68 L72 C130 N132 V133 K164 I192
Enzyme Commision number 1.3.-.-
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 B A20 A21 G22 T46 Y60 N69 M71 N128 K165 I193 N194 G220 T247 G248 G249 G270 T271 A19 A20 G21 T45 Y59 N68 M70 N127 K164 I192 N193 G219 T246 G247 G248 G269 T270
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: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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External links
PDB RCSB:3oix, PDBe:3oix, PDBj:3oix
PDBsum3oix
PubMed21301083
UniProtQ8DVA1

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