Structure of PDB 1svk Chain A Binding Site BS02

Receptor Information
>1svk Chain A (length=313) Species: 10116 (Rattus norvegicus) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
EVKLLLLGAGESGKSTIVKQMKIIHEAGYSEEECKQYKAVVYSNTIQSII
AIIRAMGRLKIDFGDAARADDARQLFVLAGAAEEGFMTAELAGVIKRLWK
DSGVQACFNRSREYQLNDSAAYYLNDLDRIAQPNYIPTQQDVLRTRVPTT
GIVETHFTFKDLHFKMFDVGGQRSERKKWIHCFEGVTAIIFCVALSDYDL
VLAEDEEMNRMHESMKLFDSICNNKWFTDTSIILFLNKKDLFEEKIKKSP
LTICYPEYAGSNTYEEAAAYIQCQFEDLNKRKDTKEIYTHFTCATDTKNV
QFVFDAVTDVIIK
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 chain1svk 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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PDB1svk Uncoupling conformational change from GTP hydrolysis in a heterotrimeric G protein {alpha}-subunit.
Resolution2.0 Å
Binding residue
(original residue number in PDB)		G42 E43 K46 R178 P180 T181 G203 Q204
Binding residue
(residue number reindexed from 1)		G10 E11 K14 R146 P148 T149 G171 Q172
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) E43 T48 R178 D200 Q204
Catalytic site (residue number reindexed from 1) E11 T16 R146 D168 Q172
Enzyme Commision number 3.6.1.46: Transferred entry: 3.6.5.1.
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:1svk, PDBe:1svk, PDBj:1svk
PDBsum1svk
PubMed15128951
UniProtP10824|GNAI1_RAT Guanine nucleotide-binding protein G(i) subunit alpha-1 (Gene Name=Gnai1)

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