Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

4JSV

mTOR kinase structure, mechanism and regulation.

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	0004674	molecular_function	protein serine/threonine kinase activity
C	0005515	molecular_function	protein binding
C	0005654	cellular_component	nucleoplasm
C	0005737	cellular_component	cytoplasm
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	0030307	biological_process	positive regulation of cell growth
C	0030674	molecular_function	protein-macromolecule adaptor activity
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	0038203	biological_process	TORC2 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	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	0004674	molecular_function	protein serine/threonine kinase activity
D	0005515	molecular_function	protein binding
D	0005654	cellular_component	nucleoplasm
D	0005737	cellular_component	cytoplasm
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	0030307	biological_process	positive regulation of cell growth
D	0030674	molecular_function	protein-macromolecule adaptor activity
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	0038203	biological_process	TORC2 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	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

Functional Information from PDB Data

site_id	AC1
Number of Residues	14
Details	BINDING SITE FOR RESIDUE ADP B 2601

Chain	Residue
B	GLN2167
B	ILE2356
B	ASP2357
B	MG2602
B	MG2603
B	MGF2604
B	LYS2187
B	GLU2190
B	ILE2237
B	GLY2238
B	TRP2239
B	VAL2240
B	THR2245
B	ASN2343

site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MG B 2602

Chain	Residue
B	ASN2343
B	ASP2357
B	ADP2601
B	MGF2604

site_id	AC3
Number of Residues	3
Details	BINDING SITE FOR RESIDUE MG B 2603

Chain	Residue
B	ASP2357
B	ADP2601
B	MGF2604

site_id	AC4
Number of Residues	7
Details	BINDING SITE FOR RESIDUE MGF B 2604

Chain	Residue
B	ASP2338
B	HIS2340
B	ASN2343
B	ASP2357
B	ADP2601
B	MG2602
B	MG2603

site_id	AC5
Number of Residues	11
Details	BINDING SITE FOR RESIDUE ADP A 2601

Chain	Residue
A	GLN2167
A	LYS2187
A	ILE2237
A	GLY2238
A	TRP2239
A	VAL2240
A	THR2245
A	ILE2356
A	ASP2357
A	MG2602
A	MGF2604

site_id	AC6
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG A 2602

Chain	Residue
A	SER2342
A	ASN2343
A	ASP2357
A	ADP2601
A	MGF2604

site_id	AC7
Number of Residues	2
Details	BINDING SITE FOR RESIDUE MG A 2603

Chain	Residue
A	ASP2357
A	MGF2604

site_id	AC8
Number of Residues	7
Details	BINDING SITE FOR RESIDUE MGF A 2604

Chain	Residue
A	ASP2338
A	HIS2340
A	ASN2343
A	ASP2357
A	ADP2601
A	MG2602
A	MG2603

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	66
Details	Repeat: {"description":"TPR 3"}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	60
Details	Repeat: {"description":"TPR 4"}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	66
Details	Repeat: {"description":"TPR 5"}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	66
Details	Repeat: {"description":"TPR 6"}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	64
Details	Repeat: {"description":"TPR 7"}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	78
Details	Repeat: {"description":"TPR 8"}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	68
Details	Repeat: {"description":"TPR 9"}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	86
Details	Repeat: {"description":"TPR 10"}

Chain

Residue

Details

site_id	SWS_FT_FI9
Number of Residues	74
Details	Repeat: {"description":"TPR 11"}

Chain

Residue

Details

site_id	SWS_FT_FI10
Number of Residues	108
Details	Repeat: {"description":"TPR 12"}

Chain

Residue

Details

site_id	SWS_FT_FI11
Number of Residues	64
Details	Repeat: {"description":"TPR 14"}

Chain

Residue

Details

site_id	SWS_FT_FI12
Number of Residues	78
Details	Repeat: {"description":"TPR 15"}

Chain

Residue

Details

site_id	SWS_FT_FI13
Number of Residues	68
Details	Repeat: {"description":"TPR 16"}

Chain

Residue

Details

site_id	SWS_FT_FI14
Number of Residues	64
Details	Domain: {"description":"FATC","evidences":[{"source":"PROSITE-ProRule","id":"PRU00534","evidenceCode":"ECO:0000255"},{"source":"PROSITE-ProRule","id":"PRU00535","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI15
Number of Residues	264
Details	Region: {"description":"Sufficient for interaction with the FKBP1A/rapamycin complex","evidences":[{"source":"UniProtKB","id":"Q9JLN9","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI16
Number of Residues	12
Details	Region: {"description":"G-loop","evidences":[{"source":"PROSITE-ProRule","id":"PRU00269","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI17
Number of Residues	76
Details	Region: {"description":"Interaction with MLST8"}

Chain

Residue

Details

site_id	SWS_FT_FI18
Number of Residues	16
Details	Region: {"description":"Catalytic loop","evidences":[{"source":"PROSITE-ProRule","id":"PRU00269","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI19
Number of Residues	50
Details	Region: {"description":"Activation loop","evidences":[{"source":"PROSITE-ProRule","id":"PRU00269","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI20
Number of Residues	6
Details	Binding site: {"evidences":[{"source":"PubMed","id":"33158864","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6ZWM","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI21
Number of Residues	22
Details	Binding site: {"evidences":[{"source":"PubMed","id":"29236692","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6BCU","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6BCX","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI22
Number of Residues	6
Details	Binding site: {"evidences":[{"source":"PubMed","id":"29236692","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6BCX","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI23
Number of Residues	2
Details	Modified residue: {"description":"Phosphoserine; by TBK1","evidences":[{"source":"PubMed","id":"21576368","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"29150432","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI24
Number of Residues	2
Details	Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"21576368","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI25
Number of Residues	2
Details	Modified residue: {"description":"Phosphothreonine; by PKB/AKT1","evidences":[{"source":"PubMed","id":"24247430","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI26
Number of Residues	4
Details	Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"PubMed","id":"37979583","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI27
Number of Residues	80
Details	Repeat: {"description":"WD 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00221","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"23636326","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI28
Number of Residues	78
Details	Repeat: {"description":"WD 3","evidences":[{"source":"PROSITE-ProRule","id":"PRU00221","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"23636326","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI29
Number of Residues	78
Details	Repeat: {"description":"WD 4","evidences":[{"source":"PROSITE-ProRule","id":"PRU00221","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"23636326","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI30
Number of Residues	78
Details	Repeat: {"description":"WD 5","evidences":[{"source":"PROSITE-ProRule","id":"PRU00221","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"23636326","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI31
Number of Residues	78
Details	Repeat: {"description":"WD 6","evidences":[{"source":"PROSITE-ProRule","id":"PRU00221","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"23636326","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI32
Number of Residues	82
Details	Repeat: {"description":"WD 7","evidences":[{"source":"PROSITE-ProRule","id":"PRU00221","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"23636326","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI33
Number of Residues	2
Details	Modified residue: {"description":"Phosphothreonine; by CDK1","evidences":[{"source":"PubMed","id":"34741373","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI34
Number of Residues	8
Details	Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO3)","evidences":[{"source":"PubMed","id":"38395307","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI35
Number of Residues	6
Details	Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate","evidences":[{"source":"PubMed","id":"28489822","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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