Structure of PDB 1jub Chain B Binding Site BS02

Receptor Information
>1jub Chain B (length=311) Species: 1358 (Lactococcus lactis) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
MLNTTFANAKFANPFMNASGVHCMTIEDLEELKASQAGAYITKSSTLEKR
EGNPLPRYVDLELGSINSMGLPNLGFDYYLDYVLKNQKENAQEGPIFFSI
AGMSAAENIAMLKKIQESDFSGITELNLSCPNVPGEPQLAYDFEATEKLL
KEVFTFFTKPLGVKLPPYFDLVHFDIMAEILNQFPLTYVNSVNSIGNGLF
IDPEAESVVIKPKDGFGGIGGAYIKPTALANVRAFYTRLKPEIQIIGTGG
IETGQDAFEHLLCGATMLQIGTALHKEGPAIFDRIIKELEEIMNQKGYQS
IADFHGKLKSL
Ligand information
Ligand IDFMN
InChIInChI=1S/C17H21N4O9P/c1-7-3-9-10(4-8(7)2)21(15-13(18-9)16(25)20-17(26)19-15)5-11(22)14(24)12(23)6-30-31(27,28)29/h3-4,11-12,14,22-24H,5-6H2,1-2H3,(H,20,25,26)(H2,27,28,29)/t11-,12+,14-/m0/s1
InChIKeyFVTCRASFADXXNN-SCRDCRAPSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.7.6Cc1cc2c(cc1C)N(C3=NC(=O)NC(=O)C3=N2)CC(C(C(COP(=O)(O)O)O)O)O
OpenEye OEToolkits 1.7.6Cc1cc2c(cc1C)N(C3=NC(=O)NC(=O)C3=N2)C[C@@H]([C@@H]([C@@H](COP(=O)(O)O)O)O)O
ACDLabs 12.01N=2C(=O)NC(=O)C3=Nc1cc(C)c(C)cc1N(C=23)CC(O)C(O)C(O)COP(=O)(O)O
CACTVS 3.385Cc1cc2N=C3C(=O)NC(=O)N=C3N(C[CH](O)[CH](O)[CH](O)CO[P](O)(O)=O)c2cc1C
CACTVS 3.385Cc1cc2N=C3C(=O)NC(=O)N=C3N(C[C@H](O)[C@H](O)[C@H](O)CO[P](O)(O)=O)c2cc1C
FormulaC17 H21 N4 O9 P
NameFLAVIN MONONUCLEOTIDE;
RIBOFLAVIN MONOPHOSPHATE
ChEMBLCHEMBL1201794
DrugBankDB03247
ZINCZINC000003831425
PDB chain1jub Chain B Residue 1800 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

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PDB1jub Lactococcus lactis dihydroorotate dehydrogenase A mutants reveal important facets of the enzymatic function
Resolution1.4 Å
Binding residue
(original residue number in PDB)		A18 S19 G20 K43 S44 N67 M69 N127 K164 N193 G221 I224 T248 G249 G250 G271 T272
Binding residue
(residue number reindexed from 1)		A18 S19 G20 K43 S44 N67 M69 N127 K164 N193 G221 I224 T248 G249 G250 G271 T272
Annotation score1
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).
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:1jub, PDBe:1jub, PDBj:1jub
PDBsum1jub
PubMed12732650
UniProtA2RJT9|PYRDA_LACLM Dihydroorotate dehydrogenase A (fumarate) (Gene Name=pyrDA)

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