Structure of PDB 4g5q Chain A Binding Site BS01

Receptor Information
>4g5q Chain A (length=320) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
AREVKLLLLGAGESGKSTIVKQMKIIHEAGYSEEECKQYKAVVYSNTIQS
IIAIIRAMGRLKIDFGDSARADDARQLFVLAGAAEEGFMTAELAGVIKRL
WKDSGVQACFNRSREYQLNDSAAYYLNDLDRIAQPNYIPTQQDVLRTRVK
TTGIVETHFTFKDLHFKMFDVGGQRSERKKWIHCFEGVTAIIFCVALSDY
DLVLAEDEEMNRMHESMKLFDSICNNKWFTDTSIILFLNKKDLFEEKIKK
SPLTICYPEYAGSNTYEEAAAYIQCQFEDLNKRKDTKEIYTHFTCATDTK
NVQFVFDAVTDVIIKNNLKD
Ligand information
>4g5q Chain E (length=21) Species: 10090 (Mus musculus) [Search peptide sequence] [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
DFFSLILRSQAKRMDEQRVLL
Receptor-Ligand Complex Structure
Global viewLocal viewStructure 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]
PDB4g5q Crystal Structures of the scaffolding protein LGN reveal the general mechanism by which GoLoco binding motifs inhibit the release of GDP from Galphai subunits in G-coupled heterotrimeric proteins
Resolution2.9 Å
Binding residue
(original residue number in PDB)		L39 G40 G42 E43 Q79 Q147 N149 R178 V179 K180 G202 G203 R205 W211 F215 L249 N256
Binding residue
(residue number reindexed from 1)		L9 G10 G12 E13 Q49 Q117 N119 R148 V149 K150 G172 G173 R175 W181 F185 L219 N226
Enzymatic activity
Catalytic site (original residue number in PDB) E43 T48 R178 D200 Q204
Catalytic site (residue number reindexed from 1) E13 T18 R148 D170 Q174
Enzyme Commision number ?
Gene Ontology
Molecular Function
GO:0000287 magnesium ion binding
GO:0001664 G protein-coupled receptor binding
GO:0003924 GTPase activity
GO:0003925 G protein activity
GO:0005515 protein binding
GO:0005525 GTP binding
GO:0010854 adenylate cyclase regulator activity
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: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:0007193 adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway
GO:0007198 adenylate cyclase-inhibiting serotonin receptor signaling pathway
GO:0034695 response to prostaglandin E
GO:0043434 response to peptide hormone
GO:0043949 regulation of cAMP-mediated signaling
GO:0045542 positive regulation of cholesterol biosynthetic process
GO:0051301 cell division
GO:0060236 regulation of mitotic spindle organization
GO:0072678 T cell migration
GO:1904322 cellular response to forskolin
GO:1904778 positive regulation of protein localization to cell cortex
Cellular Component
GO:0005634 nucleus
GO:0005654 nucleoplasm
GO:0005730 nucleolus
GO:0005737 cytoplasm
GO:0005765 lysosomal membrane
GO:0005813 centrosome
GO:0005829 cytosol
GO:0005834 heterotrimeric G-protein complex
GO:0005856 cytoskeleton
GO:0005886 plasma membrane
GO:0005938 cell cortex
GO:0030496 midbody
GO:0070062 extracellular exosome

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:4g5q, PDBe:4g5q, PDBj:4g5q
PDBsum4g5q
PubMed
UniProtP63096|GNAI1_HUMAN Guanine nucleotide-binding protein G(i) subunit alpha-1 (Gene Name=GNAI1)

[Back to BioLiP]