Structure of PDB 5urs Chain E Binding Site BS02

Receptor Information
>5urs Chain E (length=350) Species: 1392 (Bacillus anthracis) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
FQSNAMWESKFVKEGLTFDDVLLVPAKSDVLPREVSVKTVLSESLQLNIP
LISAGMDTVTEADMAIAMARQGGLGIIHKNMSIEQQAEQVDKVKRSGGLL
VGAAVGVTADAMTRIDALVKASVDAIVLDTAHGHSQGVIDKVKEVRAKYP
SLNIIAGNVATAEATKALIEAGANVVKVGIGPGSICTTRVVAGVGVPQLT
AVYDCATEARKHGIPVIADGGIKYSGDMVKALAAGAHVVMLGSMFAGVAE
SPGETEIYQGRQFKVYRGMGSVGAMEKVPEGIEGRVPYKGPLADTVHQLV
GGLRAGMGYCGAQDLEFLRENAQFIRMSGAGLLESHPHHVQITKEAPNYS
Ligand information
Ligand ID8LA
InChIInChI=1S/C24H29ClN2O6/c1-13(2)14-6-5-7-15(10-14)24(3,4)27-23(31)26-16-8-9-17(25)18(11-16)32-22-21(30)20(29)19(12-28)33-22/h5-11,19-22,28-30H,1,12H2,2-4H3,(H2,26,27,31)/t19-,20-,21-,22+/m1/s1
InChIKeyDGCHEIBDGDMRPM-YSFYHYPLSA-N
SMILES
SoftwareSMILES
CACTVS 3.385CC(=C)c1cccc(c1)C(C)(C)NC(=O)Nc2ccc(Cl)c(O[CH]3O[CH](CO)[CH](O)[CH]3O)c2
OpenEye OEToolkits 2.0.6CC(=C)c1cccc(c1)C(C)(C)NC(=O)Nc2ccc(c(c2)OC3C(C(C(O3)CO)O)O)Cl
OpenEye OEToolkits 2.0.6CC(=C)c1cccc(c1)C(C)(C)NC(=O)Nc2ccc(c(c2)O[C@@H]3[C@@H]([C@@H]([C@H](O3)CO)O)O)Cl
CACTVS 3.385CC(=C)c1cccc(c1)C(C)(C)NC(=O)Nc2ccc(Cl)c(O[C@H]3O[C@H](CO)[C@@H](O)[C@H]3O)c2
ACDLabs 12.01c3(C(C)(C)NC(=O)Nc1ccc(c(c1)OC2C(O)C(O)C(CO)O2)Cl)cccc(c3)/C(C)=C
FormulaC24 H29 Cl N2 O6
NameN-[4-chloro-3-(alpha-D-ribofuranosyloxy)phenyl]-N'-{2-[3-(prop-1-en-2-yl)phenyl]propan-2-yl}urea
ChEMBL
DrugBank
ZINCZINC000584905491
PDB chain5urs Chain E Residue 502 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB5urs Crystal Structure of the Catalytic Domain of the Inosine Monophosphate Dehydrogenase from Bacillus anthracis in the complex with IMP and the inhibitor P178
Resolution2.388 Å
Binding residue
(original residue number in PDB)		T252 A253 H254 S257 G259 V260 M391 G392 M397 E416
Binding residue
(residue number reindexed from 1)		T130 A131 H132 S135 G137 V138 M269 G270 M275 E280
Annotation score1
Enzymatic activity
Enzyme Commision number 1.1.1.205: IMP dehydrogenase.
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0003938 IMP dehydrogenase activity
GO:0016491 oxidoreductase activity
Biological Process
GO:0006164 purine nucleotide biosynthetic process

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Molecular Function
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Biological Process
External links
PDB RCSB:5urs, PDBe:5urs, PDBj:5urs
PDBsum5urs
PubMed
UniProtA0A6L8P2U9

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