Structure of PDB 1svk Chain A Binding Site BS01
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 ID
MG
InChI
InChI=1S/Mg/q+2
InChIKey
JLVVSXFLKOJNIY-UHFFFAOYSA-N
SMILES
Software
SMILES
ACDLabs 10.04
OpenEye OEToolkits 1.5.0
[Mg+2]
CACTVS 3.341
[Mg++]
Formula
Mg
Name
MAGNESIUM ION
ChEMBL
DrugBank
DB01378
ZINC
PDB chain
1svk Chain A Residue 356 [
Download ligand structure
] [
Download structure with residue number starting from 1
] [
View ligand structure
]
Receptor-Ligand Complex Structure
Global view
Local view
Structure summary
[
Spin on
] [
Spin off
] [
Reset
]
[
High quality
] [
Low quality
]
[
White background
] [
Black background
]
[
Spin on
] [
Spin off
] [
Reset
]
[
High quality
] [
Low quality
]
[
White background
] [
Black background
]
PDB
1svk
Uncoupling conformational change from GTP hydrolysis in a heterotrimeric G protein {alpha}-subunit.
Resolution
2.0 Å
Binding residue
(original residue number in PDB)
S47 T181
Binding residue
(residue number reindexed from 1)
S15 T149
Annotation score
1
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
View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB
RCSB:1svk
,
PDBe:1svk
,
PDBj:1svk
PDBsum
1svk
PubMed
15128951
UniProt
P10824
|GNAI1_RAT Guanine nucleotide-binding protein G(i) subunit alpha-1 (Gene Name=Gnai1)
[
Back to BioLiP
]