Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

5WBY

Crystal structure of mTOR(deltaN)-mLST8-PRAS40(beta-strand) complex

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004674	molecular_function	protein serine/threonine kinase activity
A	0016301	molecular_function	kinase activity
A	0044877	molecular_function	protein-containing complex binding
B	0004674	molecular_function	protein serine/threonine kinase activity
B	0016301	molecular_function	kinase activity
B	0044877	molecular_function	protein-containing complex binding
C	0005515	molecular_function	protein binding
C	0005654	cellular_component	nucleoplasm
C	0005737	cellular_component	cytoplasm
C	0005764	cellular_component	lysosome
C	0005765	cellular_component	lysosomal membrane
C	0005829	cellular_component	cytosol
C	0006974	biological_process	DNA damage response
C	0007010	biological_process	cytoskeleton organization
C	0010507	biological_process	negative regulation of autophagy
C	0016020	cellular_component	membrane
C	0030307	biological_process	positive regulation of cell growth
C	0030838	biological_process	positive regulation of actin filament polymerization
C	0031669	biological_process	cellular response to nutrient levels
C	0031929	biological_process	TOR signaling
C	0031931	cellular_component	TORC1 complex
C	0031932	cellular_component	TORC2 complex
C	0032008	biological_process	positive regulation of TOR signaling
C	0032956	biological_process	regulation of actin cytoskeleton organization
C	0038202	biological_process	TORC1 signaling
C	0043066	biological_process	negative regulation of apoptotic process
C	0043539	molecular_function	protein serine/threonine kinase activator activity
C	0045821	biological_process	positive regulation of glycolytic process
C	0046889	biological_process	positive regulation of lipid biosynthetic process
C	0050731	biological_process	positive regulation of peptidyl-tyrosine phosphorylation
C	0071456	biological_process	cellular response to hypoxia
C	0071470	biological_process	cellular response to osmotic stress
C	1905857	biological_process	positive regulation of pentose-phosphate shunt
D	0005515	molecular_function	protein binding
D	0005654	cellular_component	nucleoplasm
D	0005737	cellular_component	cytoplasm
D	0005764	cellular_component	lysosome
D	0005765	cellular_component	lysosomal membrane
D	0005829	cellular_component	cytosol
D	0006974	biological_process	DNA damage response
D	0007010	biological_process	cytoskeleton organization
D	0010507	biological_process	negative regulation of autophagy
D	0016020	cellular_component	membrane
D	0030307	biological_process	positive regulation of cell growth
D	0030838	biological_process	positive regulation of actin filament polymerization
D	0031669	biological_process	cellular response to nutrient levels
D	0031929	biological_process	TOR signaling
D	0031931	cellular_component	TORC1 complex
D	0031932	cellular_component	TORC2 complex
D	0032008	biological_process	positive regulation of TOR signaling
D	0032956	biological_process	regulation of actin cytoskeleton organization
D	0038202	biological_process	TORC1 signaling
D	0043066	biological_process	negative regulation of apoptotic process
D	0043539	molecular_function	protein serine/threonine kinase activator activity
D	0045821	biological_process	positive regulation of glycolytic process
D	0046889	biological_process	positive regulation of lipid biosynthetic process
D	0050731	biological_process	positive regulation of peptidyl-tyrosine phosphorylation
D	0071456	biological_process	cellular response to hypoxia
D	0071470	biological_process	cellular response to osmotic stress
D	1905857	biological_process	positive regulation of pentose-phosphate shunt
O	0032007	biological_process	negative regulation of TOR signaling
O	0048011	biological_process	neurotrophin TRK receptor signaling pathway
P	0032007	biological_process	negative regulation of TOR signaling
P	0048011	biological_process	neurotrophin TRK receptor signaling pathway

Functional Information from PROSITE/UniProt

site_id	PS00678
Number of Residues	15
Details	WD_REPEATS_1 Trp-Asp (WD) repeats signature. MYTGgeDcTARIWDL

Chain	Residue	Details
D	MET100-LEU114

site_id	PS00915
Number of Residues	15
Details	PI3_4_KINASE_1 Phosphatidylinositol 3- and 4-kinases signature 1. LKgh.EDLRQDervmQ

Chain	Residue	Details
B	LEU2186-GLN2200

site_id	PS00916
Number of Residues	21
Details	PI3_4_KINASE_2 Phosphatidylinositol 3- and 4-kinases signature 2. SlAvmsMvgYILgLgDRHpsN

Chain	Residue	Details
B	SER2323-ASN2343

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	MOD_RES: Phosphoserine => ECO:0000250\|UniProtKB:Q9D1F4

Chain	Residue	Details
P	SER116
B	MET2345
B	ILE2356
A	SER2165
A	GLN2167
A	LEU2185
A	GLU2190
A	TYR2225
A	GLY2238
A	TRP2239
A	VAL2240
O	SER116
A	THR2245
A	MET2345
A	ILE2356
B	LEU2185
B	GLU2190
B	TYR2225
B	GLY2238
B	TRP2239
B	VAL2240
B	THR2245

site_id	SWS_FT_FI2
Number of Residues	2
Details	MOD_RES: Phosphoserine; by MTOR => ECO:0000269\|PubMed:17517883, ECO:0000269\|PubMed:18372248, ECO:0007744\|PubMed:17081983, ECO:0007744\|PubMed:18669648, ECO:0007744\|PubMed:19690332, ECO:0007744\|PubMed:20068231, ECO:0007744\|PubMed:21406692, ECO:0007744\|PubMed:23186163

Chain	Residue	Details
P	SER183
O	SER183
B	ASP2357
A	LYS2187
A	ASN2343
A	ASP2357

site_id	SWS_FT_FI3
Number of Residues	2
Details	MOD_RES: Phosphoserine => ECO:0007744\|PubMed:18669648, ECO:0007744\|PubMed:19690332, ECO:0007744\|PubMed:20068231, ECO:0007744\|PubMed:24275569

Chain	Residue	Details
P	SER202
O	SER202

site_id	SWS_FT_FI4
Number of Residues	2
Details	MOD_RES: Phosphoserine => ECO:0007744\|PubMed:18669648, ECO:0007744\|PubMed:20068231, ECO:0007744\|PubMed:23186163, ECO:0007744\|PubMed:24275569

Chain	Residue	Details
P	SER203
O	SER203

site_id	SWS_FT_FI5
Number of Residues	2
Details	MOD_RES: Phosphothreonine; by PKB/AKT1 => ECO:0000269\|PubMed:24247430

Chain	Residue	Details
B	THR2173
A	THR2173

site_id	SWS_FT_FI6
Number of Residues	2
Details	MOD_RES: Phosphothreonine; by RPS6KB1 => ECO:0000269\|PubMed:15905173

Chain	Residue	Details
B	THR2446
A	THR2446

site_id	SWS_FT_FI7
Number of Residues	2
Details	MOD_RES: Phosphoserine; by RPS6KB1 => ECO:0000269\|PubMed:15905173, ECO:0000269\|PubMed:19145465, ECO:0007744\|PubMed:24275569

Chain	Residue	Details
B	SER2448
A	SER2448

site_id	SWS_FT_FI8
Number of Residues	2
Details	MOD_RES: Phosphoserine => ECO:0007744\|PubMed:18669648

Chain	Residue	Details
B	SER2478
A	SER2478

site_id	SWS_FT_FI9
Number of Residues	2
Details	MOD_RES: Phosphoserine; by autocatalysis => ECO:0000269\|PubMed:21576368, ECO:0007744\|PubMed:18669648

Chain	Residue	Details
B	SER2481
A	SER2481

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)