Structure of PDB 7mtx Chain D Binding Site BS03

Receptor Information
>7mtx Chain D (length=351) Species: 1392 (Bacillus anthracis) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
SNAMWESKFVKEGLTFDDVLLVPAKSDVLPREVSVKTVLSESLQLNIPLI
SAGMDTVTEADMAIAMARQGGLGIIHKNMSIEQQAEQVDKVKRSGGLLVG
AAVGVTADAMTRIDALVKASVDAIVLDTAHGHSQGVIDKVKEVRAKYPSL
NIIAGNVATAEATKALIEAGANVVKVGIGPGSICTTRVVAGVGVPQLTAV
YDCATEARKHGIPVIADGGIKYSGDMVKALAAGAHVVMLGSMFAGVAESP
GETEIYQGRQFKVYRGMGSVGAMEKGKLVPEGIEGRVPYKGPLADTVHQL
VGGLRAGMGYCGAQDLEFLRENAQFIRMSGAGLLESHPHHVQITKEAPNY
S
Ligand information
Ligand IDZO4
InChIInChI=1S/C24H30ClN3O5/c1-13(2)14-6-5-7-15(10-14)24(3,4)28-23(32)26-16-8-9-17(25)18(11-16)27-22-21(31)20(30)19(29)12-33-22/h5-11,19-22,27,29-31H,1,12H2,2-4H3,(H2,26,28,32)/t19-,20-,21-,22-/m1/s1
InChIKeyAFRUCARRYXUVSH-GXRSIYKFSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 2.0.7CC(=C)c1cccc(c1)C(C)(C)NC(=O)Nc2ccc(c(c2)N[C@H]3[C@@H]([C@@H]([C@@H](CO3)O)O)O)Cl
ACDLabs 12.01C=C(C)c1cccc(c1)C(C)(C)NC(=O)Nc1cc(NC2OCC(O)C(O)C2O)c(Cl)cc1
CACTVS 3.385CC(=C)c1cccc(c1)C(C)(C)NC(=O)Nc2ccc(Cl)c(N[C@@H]3OC[C@@H](O)[C@@H](O)[C@H]3O)c2
OpenEye OEToolkits 2.0.7CC(=C)c1cccc(c1)C(C)(C)NC(=O)Nc2ccc(c(c2)NC3C(C(C(CO3)O)O)O)Cl
CACTVS 3.385CC(=C)c1cccc(c1)C(C)(C)NC(=O)Nc2ccc(Cl)c(N[CH]3OC[CH](O)[CH](O)[CH]3O)c2
FormulaC24 H30 Cl N3 O5
NameN-{2-chloro-5-[({2-[3-(prop-1-en-2-yl)phenyl]propan-2-yl}carbamoyl)amino]phenyl}-beta-D-ribopyranosylamine
ChEMBL
DrugBank
ZINC
PDB chain7mtx Chain D Residue 503 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB7mtx Crystal Structure of the Catalytic Domain of the Inosine Monophosphate Dehydrogenase from Bacillus anthracis in the complex with IMP and the inhibitor P176
Resolution2.44 Å
Binding residue
(original residue number in PDB)		T252 A253 H254 G392 E416
Binding residue
(residue number reindexed from 1)		T128 A129 H130 G268 E281
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

View graph for
Molecular Function
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Biological Process
External links
PDB RCSB:7mtx, PDBe:7mtx, PDBj:7mtx
PDBsum7mtx
PubMed
UniProtA0A6L8P2U9

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