Structure of PDB 2g83 Chain B

Receptor sequence
>2g83B (length=303) Species: 9606 (Homo sapiens) [Search protein sequence]
EVKLLLLGAGESGKSTIVKQMKIIHEAGYSEEECKQYKAVVYSNTIQSII
AIIRAMGRLKIDFGDSARADDARQLFVLAELAGVIKRLWKDSGVQACFNR
SREYQLNDSAAYYLNDLDRIAQPNYIPTQQDVLRTRVKTTGIVETHFTFK
DLHFKMFDVGGQRSERKKWIHCFEGVTAIIFCVALSDYDLVLAEDEEMNR
MHESMKLFDSICNNKWFTDTSIILFLNKKDLFEEKIKKSPLTICYPEYAG
SNTYEEAAAYIQCQFEDLNKRKDTKEIYTHFTCATDTKNVQFVFDAVTDV
IIK
3D structure
PDB2g83 Minimal Determinants for Binding Activated Galpha from the Structure of a Galpha(i1)-Peptide Dimer.
ChainB
Resolution2.8 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) E43 T48 R178 D200 Q204
Catalytic site (residue number reindexed from 1) E11 T16 R136 D158 Q162
Enzyme Commision number ?
Interaction with ligand
Site
#
Ligand Ligand
chain
Binding residues on receptor
(original residue number in PDB)
Binding residues on receptor
(residue number reindexed from 1)
Binding affinity
BS01 peptide B R205 R208 F215 E245 K248 S252 R163 R166 F173 E203 K206 S210
BS02 ALF B G42 E43 R178 T181 Q204 G10 E11 R136 T139 Q162
BS03 MG B S47 T181 S15 T139
BS04 GDP B E43 G45 K46 S47 T48 R176 R178 K270 D272 C325 T327 E11 G13 K14 S15 T16 R134 R136 K228 D230 C283 T285
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:2g83, PDBe:2g83, PDBj:2g83
PDBsum2g83
PubMed16981699
UniProtP63096|GNAI1_HUMAN Guanine nucleotide-binding protein G(i) subunit alpha-1 (Gene Name=GNAI1)

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