Structure of PDB 1bh2 Chain A Binding Site BS01
Receptor Information
>1bh2 Chain A (length=315) Species:
10116
(Rattus norvegicus) [
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REVKLLLLGAGESGKSTIVKQMKIIHEAGYSEEECKQYKAVVYSNTIQSI
IAIIRAMGRLKIDFGDAARADDARQLFVLAGAAEEGFMTAELAGVIKRLW
KDSGVQACFNRSREYQLNDSAAYYLNDLDRIAQPNYIPTQQDVLRTRVKT
TGIVETHFTFKDLHFKMFDVGGQRSERKKWIHCFEGVTAIIFCVALSDYD
LVLAEDEEMNRMHESMKLFDSICNNKWFTDTSIILFLNKKDLFEEKIKKS
PLTICYPEYAGSNTYEEAAAYIQCQFEDLNKRKDTKEIYTHFTCSTDTKN
VQFVFDAVTDVIIKN
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
1bh2 Chain A Residue 357 [
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Receptor-Ligand Complex Structure
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PDB
1bh2
The A326S mutant of Gialpha1 as an approximation of the receptor-bound state.
Resolution
2.1 Å
Binding residue
(original residue number in PDB)
S47 T181
Binding residue
(residue number reindexed from 1)
S16 T150
Annotation score
1
Enzymatic activity
Catalytic site (original residue number in PDB)
E43 T48 R178 D200 Q204
Catalytic site (residue number reindexed from 1)
E12 T17 R147 D169 Q173
Enzyme Commision number
?
Gene Ontology
Molecular Function
GO:0003924
GTPase activity
GO:0005525
GTP binding
GO:0019001
guanyl nucleotide binding
GO:0031683
G-protein beta/gamma-subunit complex 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
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Molecular Function
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Biological Process
External links
PDB
RCSB:1bh2
,
PDBe:1bh2
,
PDBj:1bh2
PDBsum
1bh2
PubMed
9705312
UniProt
P10824
|GNAI1_RAT Guanine nucleotide-binding protein G(i) subunit alpha-1 (Gene Name=Gnai1)
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