Structure of PDB 4g5r Chain D Binding Site BS02

Receptor Information
>4g5r Chain D (length=317) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
KEVKLLLLGAGESGKSTIVKQMKIIHEDGYSEDECKQYKVVVYSNTIQSI
IAIIRAMGRLKIDFGEAARADDARQLFVLAGSAEEGVMTPELAGVIKRLW
RDGGVQACFSRSREYQLNDSASYYLNDLDRISQSNYIPTQQDVLRTRVKT
TGIVETHFTFKDLYFKMFDVERKKWIHCFEGVTAIIFCVALSDYDLVLAE
DEEMNRMHESMKLFDSICNNKWFTETSIILFLNKKDLFEEKIKRSPLTIC
YPEYTGSNTYEEAAAYIQCQFEDLNRRKDTKEIYTHFTCATDTKNVQFVF
DAVTDVIIKNNLKECGL
Ligand information
Ligand IDGDP
InChIInChI=1S/C10H15N5O11P2/c11-10-13-7-4(8(18)14-10)12-2-15(7)9-6(17)5(16)3(25-9)1-24-28(22,23)26-27(19,20)21/h2-3,5-6,9,16-17H,1H2,(H,22,23)(H2,19,20,21)(H3,11,13,14,18)/t3-,5-,6-,9-/m1/s1
InChIKeyQGWNDRXFNXRZMB-UUOKFMHZSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.7.6c1nc2c(n1C3C(C(C(O3)COP(=O)(O)OP(=O)(O)O)O)O)N=C(NC2=O)N
CACTVS 3.385NC1=Nc2n(cnc2C(=O)N1)[C@@H]3O[C@H](CO[P](O)(=O)O[P](O)(O)=O)[C@@H](O)[C@H]3O
CACTVS 3.385NC1=Nc2n(cnc2C(=O)N1)[CH]3O[CH](CO[P](O)(=O)O[P](O)(O)=O)[CH](O)[CH]3O
ACDLabs 12.01O=P(O)(O)OP(=O)(O)OCC3OC(n2cnc1c2N=C(N)NC1=O)C(O)C3O
OpenEye OEToolkits 1.7.6c1nc2c(n1[C@H]3[C@@H]([C@@H]([C@H](O3)CO[P@](=O)(O)OP(=O)(O)O)O)O)N=C(NC2=O)N
FormulaC10 H15 N5 O11 P2
NameGUANOSINE-5'-DIPHOSPHATE
ChEMBLCHEMBL384759
DrugBankDB04315
ZINCZINC000008215481
PDB chain4g5r Chain D Residue 401 [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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PDB4g5r Crystal Structures of the scaffolding protein LGN reveal the general mechanism by which GoLoco binding motifs inhibit the release of GDP from Galphai subunits in G-coupled heterotrimeric proteins
Resolution3.481 Å
Binding residue
(original residue number in PDB)		E43 S44 G45 K46 S47 T48 D150 S151 R176 R178 N269 K270 D272 L273 C325 A326 T327
Binding residue
(residue number reindexed from 1)		E12 S13 G14 K15 S16 T17 D119 S120 R145 R147 N233 K234 D236 L237 C289 A290 T291
Annotation score4
Enzymatic activity
Catalytic site (original residue number in PDB) E43 T48 R178 D200
Catalytic site (residue number reindexed from 1) E12 T17 R147 D169
Enzyme Commision number ?
Gene Ontology
Molecular Function
GO:0001664 G protein-coupled receptor binding
GO:0003924 GTPase activity
GO:0005515 protein binding
GO:0005525 GTP binding
GO:0019001 guanyl nucleotide binding
GO:0019003 GDP binding
GO:0031683 G-protein beta/gamma-subunit complex binding
GO:0046872 metal ion binding
Biological Process
GO:0007165 signal transduction
GO:0007186 G protein-coupled receptor signaling pathway
GO:0007188 adenylate cyclase-modulating G protein-coupled receptor signaling pathway
GO:0007193 adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway
GO:0007194 negative regulation of adenylate cyclase activity
GO:0007212 G protein-coupled dopamine receptor signaling pathway
GO:0016239 positive regulation of macroautophagy
GO:0046039 GTP metabolic process
GO:0051301 cell division
Cellular Component
GO:0000139 Golgi membrane
GO:0005654 nucleoplasm
GO:0005730 nucleolus
GO:0005737 cytoplasm
GO:0005765 lysosomal membrane
GO:0005789 endoplasmic reticulum membrane
GO:0005794 Golgi apparatus
GO:0005813 centrosome
GO:0005834 heterotrimeric G-protein complex
GO:0005856 cytoskeleton
GO:0005886 plasma membrane
GO:0016020 membrane
GO:0030496 midbody
GO:0070062 extracellular exosome

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:4g5r, PDBe:4g5r, PDBj:4g5r
PDBsum4g5r
PubMed
UniProtP08754|GNAI3_HUMAN Guanine nucleotide-binding protein G(i) subunit alpha-3 (Gene Name=GNAI3)

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