Structure of PDB 3d7m Chain A Binding Site BS02

Receptor Information
>3d7m Chain A (length=305) Species: 10116 (Rattus norvegicus) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
VKLLLLGAGESGKSTIVKQMKICHEAGYSEEECKQYKAVVYSNTIQSIIA
IIRAMGRLKIDFGDAARADDARQLFVLAAELAGVIKRLWKDSGVQACFNR
SREYQLNDSAAYYLNDLDRIAQPNYIPTQQDVLRTRVKTTGIVETHFTFK
DLHFKMFDVGGQRSERKKWIHCFEGVTAIIFCVALSDYDLVLAEDEEMNR
MHESMKLFDSICNNKWFTDTSIILFLNKKDLFEEKIKKSPLTICYPEYAG
SNTYEEAAAYIQCQFEDLNKRKDTKEIYTHFTCATDTKNVCFVFDAVTDV
IIKNN
Ligand information
Ligand IDALF
InChIInChI=1S/Al.4FH/h;4*1H/q+3;;;;/p-4
InChIKeyUYOMQIYKOOHAMK-UHFFFAOYSA-J
SMILES
SoftwareSMILES
ACDLabs 10.04
CACTVS 3.341
OpenEye OEToolkits 1.5.0		F[Al-](F)(F)F
FormulaAl F4
NameTETRAFLUOROALUMINATE ION
ChEMBL
DrugBankDB04444
ZINC
PDB chain3d7m Chain A Residue 357 [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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PDB3d7m Helix dipole movement and conformational variability contribute to allosteric GDP release in Galphai subunits.
Resolution2.9 Å
Binding residue
(original residue number in PDB)		E43 K46 R178 K180 T181 G203 Q204
Binding residue
(residue number reindexed from 1)		E10 K13 R136 K138 T139 G161 Q162
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) E43 T48 R178 D200 Q204
Catalytic site (residue number reindexed from 1) E10 T15 R136 D158 Q162
Enzyme Commision number ?
Gene Ontology
Molecular Function
GO:0000287 magnesium ion binding
GO:0001664 G protein-coupled receptor binding
GO:0003924 GTPase activity
GO:0005515 protein binding
GO:0005525 GTP binding
GO:0016787 hydrolase activity
GO:0019001 guanyl nucleotide binding
GO:0019003 GDP binding
GO:0031683 G-protein beta/gamma-subunit complex binding
GO:0031749 D2 dopamine receptor binding
GO:0031821 G protein-coupled serotonin receptor binding
GO:0032794 GTPase activating protein 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:0043949 regulation of cAMP-mediated signaling
GO:0050805 negative regulation of synaptic transmission
GO:0051301 cell division
GO:0060236 regulation of mitotic spindle organization
GO:0099645 neurotransmitter receptor localization to postsynaptic specialization membrane
GO:1904322 cellular response to forskolin
GO:1904778 positive regulation of protein localization to cell cortex
Cellular Component
GO:0005634 nucleus
GO:0005737 cytoplasm
GO:0005813 centrosome
GO:0005834 heterotrimeric G-protein complex
GO:0005856 cytoskeleton
GO:0005886 plasma membrane
GO:0005938 cell cortex
GO:0030496 midbody
GO:0032991 protein-containing complex
GO:0098794 postsynapse
GO:0098978 glutamatergic synapse

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:3d7m, PDBe:3d7m, PDBj:3d7m
PDBsum3d7m
PubMed19222191
UniProtP10824|GNAI1_RAT Guanine nucleotide-binding protein G(i) subunit alpha-1 (Gene Name=Gnai1)

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