Structure of PDB 1agr Chain A Binding Site BS02
Receptor Information
>1agr Chain A (length=350) Species:
10116
(Rattus norvegicus) [
Search protein sequence
] [
Download receptor structure
] [
Download structure with residue number starting from 1
] [
View receptor structure
]
LSAEDKAAVERSKMIDRNLREDGEKAAREVKLLLLGAGESGKSTIVKQMK
IIHEAGYSEEECKQYKAVVYSNTIQSIIAIIRAMGRLKIDFGDAARADDA
RQLFVLAGAAEEGFMTAELAGVIKRLWKDSGVQACFNRSREYQLNDSAAY
YLNDLDRIAQPNYIPTQQDVLRTRVKTTGIVETHFTFKDLHFKMFDVGGQ
RSERKKWIHCFEGVTAIIFCVALSDYDLVLAEDEEMNRMHESMKLFDSIC
NNKWFTDTSIILFLNKKDLFEEKIKKSPLTICYPEYAGSNTYEEAAAYIQ
CQFEDLNKRKDTKEIYTHFTCATDTKNVQFVFDAVTDVIIKNNLKDCGLF
Ligand information
Ligand ID
ALF
InChI
InChI=1S/Al.4FH/h;4*1H/q+3;;;;/p-4
InChIKey
UYOMQIYKOOHAMK-UHFFFAOYSA-J
SMILES
Software
SMILES
ACDLabs 10.04
CACTVS 3.341
OpenEye OEToolkits 1.5.0
F[Al-](F)(F)F
Formula
Al F4
Name
TETRAFLUOROALUMINATE ION
ChEMBL
DrugBank
DB04444
ZINC
PDB chain
1agr Chain A Residue 357 [
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
1agr
Structure of RGS4 bound to AlF4--activated G(i alpha1): stabilization of the transition state for GTP hydrolysis.
Resolution
2.8 Å
Binding residue
(original residue number in PDB)
G42 E43 K46 R178 K180 T181 G203
Binding residue
(residue number reindexed from 1)
G38 E39 K42 R174 K176 T177 G199
Annotation score
1
Enzymatic activity
Catalytic site (original residue number in PDB)
E43 T48 R178 D200 Q204
Catalytic site (residue number reindexed from 1)
E39 T44 R174 D196 Q200
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
View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB
RCSB:1agr
,
PDBe:1agr
,
PDBj:1agr
PDBsum
1agr
PubMed
9108480
UniProt
P10824
|GNAI1_RAT Guanine nucleotide-binding protein G(i) subunit alpha-1 (Gene Name=Gnai1)
[
Back to BioLiP
]