Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

5FLC

Architecture of human mTOR Complex 1 - 5.9 Angstrom reconstruction

Functional Information from GO Data

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

Functional Information from PDB Data

site_id	AC1
Number of Residues	12
Details	BINDING SITE FOR RESIDUE RAP C 999

Chain	Residue
B	GLU2032
C	UNK54
C	UNK55
C	UNK56
B	SER2035
B	ARG2036
B	PHE2039
B	GLY2040
B	TRP2101
B	TYR2105
B	PHE2108
C	UNK53

site_id	AC2
Number of Residues	12
Details	BINDING SITE FOR RESIDUE RAP G 999

Chain	Residue
F	GLU2032
F	SER2035
F	ARG2036
F	PHE2039
F	GLY2040
F	TRP2101
F	TYR2105
F	PHE2108
G	UNK53
G	UNK54
G	UNK55
G	UNK56

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: N-acetylmethionine => ECO:0007744\|PubMed:19369195, ECO:0007744\|PubMed:20068231

Chain	Residue	Details
D	MET1
B	MET2345
B	ILE2356
F	SER2165
F	GLN2167
F	LEU2185
F	GLU2190
F	TYR2225
F	GLY2238
F	TRP2239
F	VAL2240
H	MET1
F	THR2245
F	MET2345
F	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: Phosphothreonine; by CDK1 => ECO:0000269\|PubMed:34741373

Chain	Residue	Details
D	THR51
H	THR51
B	ASP2357
F	LYS2187
F	ASN2343
F	ASP2357

site_id	SWS_FT_FI3
Number of Residues	2
Details	MOD_RES: Phosphoserine; by TBK1 => ECO:0000269\|PubMed:21576368, ECO:0000269\|PubMed:29150432

Chain	Residue	Details
B	SER2159
F	SER2159

site_id	SWS_FT_FI4
Number of Residues	2
Details	MOD_RES: Phosphothreonine => ECO:0000269\|PubMed:21576368

Chain	Residue	Details
B	THR2164
F	THR2164

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
F	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
F	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
F	SER2448

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

Chain	Residue	Details
B	SER2478
F	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
F	SER2481

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)