Structure of PDB 7mtu Chain F Binding Site BS02

Receptor Information

>7mtu Chain F (length=348) Species: 1392 (Bacillus anthracis)

NAMWESKFVKEGLTFDDVLLVPAKSDVLPREVSVKTVLSESLQLNIPLIS
AGMDTVTEADMAIAMARQGGLGIIHKNMSIEQQAEQVDKVKRSGGLLVGA
AVGVTADAMTRIDALVKASVDAIVLDTAHGHSQGVIDKVKEVRAKYPSLN
IIAGNVATAEATKALIEAGANVVKVGIGPGSICTTRVVAGVGVPQLTAVY
DCATEARKHGIPVIADGGIKYSGDMVKALAAGAHVVMLGSMFAGVAESPG
ETEIYQGRQFKVYRGMGSVGAMEKLVPEGIEGRVPYKGPLADTVHQLVGG
LRAGMGYCGAQDLEFLRENAQFIRMSGAGLLESHPHHVQITKEAPNYS

Ligand information

• Ligand ID: ZO7
• InChI: InChI=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
• InChIKey: AFRUCARRYXUVSH-YUMYIRISSA-N
• SMILES:
  OpenEye OEToolkits 2.0.7: CC(=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 12.01: C=C(C)c1cccc(c1)C(C)(C)NC(=O)Nc1cc(NC2OCC(O)C(O)C2O)c(Cl)cc1
  OpenEye OEToolkits 2.0.7: CC(=C)c1cccc(c1)C(C)(C)NC(=O)Nc2ccc(c(c2)NC3C(C(C(CO3)O)O)O)Cl
  CACTVS 3.385: CC(=C)c1cccc(c1)C(C)(C)NC(=O)Nc2ccc(Cl)c(N[CH]3OC[CH](O)[CH](O)[CH]3O)c2
  CACTVS 3.385: CC(=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
• Formula: C24 H30 Cl N3 O5
• Name: N-{2-chloro-5-[({2-[3-(prop-1-en-2-yl)phenyl]propan-2-yl}carbamoyl)amino]phenyl}-beta-D-arabinopyranosylamine
• PDB chain: 7mtu Chain F Residue 502

Receptor-Ligand Complex Structure

Structure summary

• PDB: 7mtu Crystal Structure of the Catalytic Domain of the Inosine Monophosphate Dehydrogenase from Bacillus anthracis in the complex with IMP and the inhibitor P221
• Resolution: 2.34 Å
• Binding residue (original residue number in PDB): T252 A253 H254 S257 V260 M391 G392 E416
• Binding residue (residue number reindexed from 1): T127 A128 H129 S132 V135 M266 G267 E278
• Annotation score: 1

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

External links

• PDB: RCSB:7mtu, PDBe:7mtu, PDBj:7mtu
• PDBsum: 7mtu
• UniProt: A0A6L8P2U9