Structure of PDB 1b3o Chain B Binding Site BS02

Receptor Information
>1b3o Chain B (length=410) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
TSYVPDDGLTAQQLFNCGDGLTYNDFLILPGYIDFTADQVDLTSALTKKI
TLKTPLVSSPMDTVTEAGMAIAMALTGGIGFIHHNCTPEFQANEVRKVKK
YEQGFITDPVVLSPKDRVRCGIPITDTGRMGSRLVGIIIMTKREDLVVAP
AGITLKEANEILQRSKKGKLPIVNEDDELVAIIARTDLKKNRDYPLASKD
AKKQLLCGAAIGTHEDDKYRLDLLAQAGVDVVVLDSSQGNSIFQINMIKY
IKDKYPNLQVIGGNVVTAAQAKNLIDAGVDALRVGMGSGSICITQEVLAC
GRPQATAVYKVSEYARRFGVPVIADGGIQNVGHIAKALALGASTVMMGSL
LAATTEAPGEDKGSIHKFVPYLIAGIQHSCQDIGAKSLTQVRAMMYSGEL
KFEKRTSSAQ
Ligand information
Ligand IDSAE
InChIInChI=1S/C19H25N7O14P2Se/c20-15-9-17(23-4-22-15)26(5-24-9)19-13(30)11(28)8(39-19)2-37-42(34,35)40-41(32,33)36-1-7-10(27)12(29)14(38-7)18-25-6(3-43-18)16(21)31/h3-5,7-8,10-14,19,27-30H,1-2H2,(H2,21,31)(H,32,33)(H,34,35)(H2,20,22,23)/t7-,8-,10-,11-,12-,13-,14-,19-/m1/s1
InChIKeySKNBJMQZTZPCPF-QZTLEVGFSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.5.0c1c(nc([se]1)[C@H]2[C@@H]([C@@H]([C@H](O2)CO[P@@](=O)(O)O[P@@](=O)(O)OC[C@@H]3[C@H]([C@H]([C@@H](O3)n4cnc5c4ncnc5N)O)O)O)O)C(=O)N
CACTVS 3.341NC(=O)c1c[se]c(n1)[CH]2O[CH](CO[P](O)(=O)O[P](O)(=O)OC[CH]3O[CH]([CH](O)[CH]3O)n4cnc5c(N)ncnc45)[CH](O)[CH]2O
CACTVS 3.341NC(=O)c1c[se]c(n1)[C@@H]2O[C@H](CO[P@](O)(=O)O[P@](O)(=O)OC[C@H]3O[C@H]([C@H](O)[C@@H]3O)n4cnc5c(N)ncnc45)[C@@H](O)[C@H]2O
OpenEye OEToolkits 1.5.0c1c(nc([se]1)C2C(C(C(O2)COP(=O)(O)OP(=O)(O)OCC3C(C(C(O3)n4cnc5c4ncnc5N)O)O)O)O)C(=O)N
ACDLabs 10.04O=P(O)(OCC3OC(n1c2ncnc(N)c2nc1)C(O)C3O)OP(=O)(O)OCC5OC(c4nc(c[se]4)C(=O)N)C(O)C5O
FormulaC19 H25 N7 O14 P2 Se
NameSELENAZOLE-4-CARBOXYAMIDE-ADENINE DINUCLEOTIDE
ChEMBLCHEMBL451855
DrugBankDB03070
ZINC
PDB chain1b3o Chain B Residue 601 [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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PDB1b3o Crystal structure of human type II inosine monophosphate dehydrogenase: implications for ligand binding and drug design.
Resolution2.9 Å
Binding residue
(original residue number in PDB)		T252 H253 D274 S275 S276 F282 N303 Q334
Binding residue
(residue number reindexed from 1)		T213 H214 D235 S236 S237 F243 N264 Q295
Annotation score3
Enzymatic activity
Enzyme Commision number 1.1.1.205: IMP dehydrogenase.
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0003677 DNA binding
GO:0003723 RNA binding
GO:0003824 catalytic activity
GO:0003938 IMP dehydrogenase activity
GO:0005515 protein binding
GO:0016491 oxidoreductase activity
GO:0046872 metal ion binding
Biological Process
GO:0006164 purine nucleotide biosynthetic process
GO:0006177 GMP biosynthetic process
GO:0006183 GTP biosynthetic process
GO:0007623 circadian rhythm
GO:0046651 lymphocyte proliferation
GO:0071353 cellular response to interleukin-4
GO:0097294 'de novo' XMP biosynthetic process
Cellular Component
GO:0005576 extracellular region
GO:0005634 nucleus
GO:0005737 cytoplasm
GO:0005778 peroxisomal membrane
GO:0005829 cytosol
GO:0016020 membrane
GO:0034774 secretory granule lumen
GO:0070062 extracellular exosome
GO:1904813 ficolin-1-rich granule lumen

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Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:1b3o, PDBe:1b3o, PDBj:1b3o
PDBsum1b3o
PubMed10097070
UniProtP12268|IMDH2_HUMAN Inosine-5'-monophosphate dehydrogenase 2 (Gene Name=IMPDH2)

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