Structure of PDB 5wby Chain D

Receptor sequence

>5wbyD (length=317) Species: 9606 (Homo sapiens) [Search protein sequence]

VGSDPVILATAGYDHTVRFWQAHSGICTRTVQHQDSQVNALEVTPDRSMI
AAAGYQHIRMYDLNSNNPNPIISYDGVNKNIASVGFHEDGRWMYTGGEDC
TARIWDLRSRNLQCQRIFQVNAPINCVCLHPNQAELIVGDQSGAIHIWDL
KTDHNEQLIPEPEVSITSAHIDPDASYMAAVNSTGNCYVWNLTGGIGDEV
TQLIPKTKIPAHTRYALQCRFSPDSTLLATCSADQTCKIWRTSNFSLMTE
LSIKSGNPGESSRGWMWGCAFSGDSQYIVTASSDNLARLWCVETGEIKRE
YGGHQKAVVCLAFNDSV

3D structure

PDB

5wby Mechanisms of mTORC1 activation by RHEB and inhibition by PRAS40.

Chain

Resolution

3.1 Å

3D
structure

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Enzymatic activity

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	D	Q164 L165 I166 P167 Y195 V196 W197 P212 K213 T214	Q157 L158 I159 P160 Y188 V189 W190 P205 K206 T207

Gene Ontology

	Molecular Function
GO:0005515	protein binding
GO:0043539	protein serine/threonine kinase activator activity

	Biological Process
GO:0006974	DNA damage response
GO:0007010	cytoskeleton organization
GO:0010507	negative regulation of autophagy
GO:0030307	positive regulation of cell growth
GO:0030838	positive regulation of actin filament polymerization
GO:0031669	cellular response to nutrient levels
GO:0031929	TOR signaling
GO:0032008	positive regulation of TOR signaling
GO:0032956	regulation of actin cytoskeleton organization
GO:0038202	TORC1 signaling
GO:0043066	negative regulation of apoptotic process
GO:0045821	positive regulation of glycolytic process
GO:0046889	positive regulation of lipid biosynthetic process
GO:0050731	positive regulation of peptidyl-tyrosine phosphorylation
GO:0071456	cellular response to hypoxia
GO:0071470	cellular response to osmotic stress
GO:1905857	positive regulation of pentose-phosphate shunt

	Cellular Component
GO:0005654	nucleoplasm
GO:0005737	cytoplasm
GO:0005764	lysosome
GO:0005765	lysosomal membrane
GO:0005829	cytosol
GO:0016020	membrane
GO:0031931	TORC1 complex
GO:0031932	TORC2 complex

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Molecular Function

View graph for
Biological Process

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Cellular Component

External links

PDB	RCSB:5wby, PDBe:5wby, PDBj:5wby
PDBsum	5wby
PubMed	29236692
UniProt	Q9BVC4\|LST8_HUMAN Target of rapamycin complex subunit LST8 (Gene Name=MLST8)

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