Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

6CES

Cryo-EM structure of GATOR1-RAG

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003924	molecular_function	GTPase activity
A	0005515	molecular_function	protein binding
A	0005525	molecular_function	GTP binding
A	0005634	cellular_component	nucleus
A	0005654	cellular_component	nucleoplasm
A	0005737	cellular_component	cytoplasm
A	0005764	cellular_component	lysosome
A	0005765	cellular_component	lysosomal membrane
A	0005829	cellular_component	cytosol
A	0006915	biological_process	apoptotic process
A	0008104	biological_process	protein localization
A	0009267	biological_process	cellular response to starvation
A	0010507	biological_process	negative regulation of autophagy
A	0016020	cellular_component	membrane
A	0016787	molecular_function	hydrolase activity
A	0031625	molecular_function	ubiquitin protein ligase binding
A	0031669	biological_process	cellular response to nutrient levels
A	0032008	biological_process	positive regulation of TOR signaling
A	0033209	biological_process	tumor necrosis factor-mediated signaling pathway
A	0034198	biological_process	cellular response to amino acid starvation
A	0035556	biological_process	intracellular signal transduction
A	0042593	biological_process	glucose homeostasis
A	0042803	molecular_function	protein homodimerization activity
A	0043495	molecular_function	protein-membrane adaptor activity
A	0046982	molecular_function	protein heterodimerization activity
A	0051219	molecular_function	phosphoprotein binding
A	0061462	biological_process	protein localization to lysosome
A	0071230	biological_process	cellular response to amino acid stimulus
A	0072657	biological_process	protein localization to membrane
A	1904263	biological_process	positive regulation of TORC1 signaling
A	1990130	cellular_component	GATOR1 complex
A	1990131	cellular_component	Gtr1-Gtr2 GTPase complex
A	1990877	cellular_component	FNIP-folliculin RagC/D GAP
C	0000287	molecular_function	magnesium ion binding
C	0003924	molecular_function	GTPase activity
C	0005515	molecular_function	protein binding
C	0005525	molecular_function	GTP binding
C	0005634	cellular_component	nucleus
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	0006351	biological_process	DNA-templated transcription
C	0006915	biological_process	apoptotic process
C	0007264	biological_process	small GTPase-mediated signal transduction
C	0008104	biological_process	protein localization
C	0008380	biological_process	RNA splicing
C	0009267	biological_process	cellular response to starvation
C	0010507	biological_process	negative regulation of autophagy
C	0016020	cellular_component	membrane
C	0016787	molecular_function	hydrolase activity
C	0019003	molecular_function	GDP binding
C	0031669	biological_process	cellular response to nutrient levels
C	0032006	biological_process	regulation of TOR signaling
C	0034198	biological_process	cellular response to amino acid starvation
C	0043200	biological_process	response to amino acid
C	0043231	cellular_component	intracellular membrane-bounded organelle
C	0043495	molecular_function	protein-membrane adaptor activity
C	0046982	molecular_function	protein heterodimerization activity
C	0051020	molecular_function	GTPase binding
C	0060090	molecular_function	molecular adaptor activity
C	0061462	biological_process	protein localization to lysosome
C	0071230	biological_process	cellular response to amino acid stimulus
C	0072657	biological_process	protein localization to membrane
C	0140767	molecular_function	enzyme-substrate adaptor activity
C	1903432	biological_process	regulation of TORC1 signaling
C	1904263	biological_process	positive regulation of TORC1 signaling
C	1990131	cellular_component	Gtr1-Gtr2 GTPase complex
C	1990877	cellular_component	FNIP-folliculin RagC/D GAP
D	0005096	molecular_function	GTPase activator activity
D	0005737	cellular_component	cytoplasm
D	0005764	cellular_component	lysosome
D	0005765	cellular_component	lysosomal membrane
D	0005829	cellular_component	cytosol
D	0010508	biological_process	positive regulation of autophagy
D	0016020	cellular_component	membrane
D	0031267	molecular_function	small GTPase binding
D	0031463	cellular_component	Cul3-RING ubiquitin ligase complex
D	0034198	biological_process	cellular response to amino acid starvation
D	0035556	biological_process	intracellular signal transduction
D	0044877	molecular_function	protein-containing complex binding
D	0048471	cellular_component	perinuclear region of cytoplasm
D	1904262	biological_process	negative regulation of TORC1 signaling
D	1990130	cellular_component	GATOR1 complex
M	0003281	biological_process	ventricular septum development
M	0005096	molecular_function	GTPase activator activity
M	0005515	molecular_function	protein binding
M	0005764	cellular_component	lysosome
M	0005765	cellular_component	lysosomal membrane
M	0010508	biological_process	positive regulation of autophagy
M	0016020	cellular_component	membrane
M	0032007	biological_process	negative regulation of TOR signaling
M	0034198	biological_process	cellular response to amino acid starvation
M	0035909	biological_process	aorta morphogenesis
M	0038202	biological_process	TORC1 signaling
M	0048738	biological_process	cardiac muscle tissue development
M	0060021	biological_process	roof of mouth development
M	1904262	biological_process	negative regulation of TORC1 signaling
M	1990130	cellular_component	GATOR1 complex
N	0005096	molecular_function	GTPase activator activity
N	0005515	molecular_function	protein binding
N	0005764	cellular_component	lysosome
N	0005765	cellular_component	lysosomal membrane
N	0005774	cellular_component	vacuolar membrane
N	0010508	biological_process	positive regulation of autophagy
N	0016020	cellular_component	membrane
N	0033673	biological_process	negative regulation of kinase activity
N	0034198	biological_process	cellular response to amino acid starvation
N	1904262	biological_process	negative regulation of TORC1 signaling
N	1990130	cellular_component	GATOR1 complex

Functional Information from PDB Data

site_id	AC1
Number of Residues	17
Details	binding site for residue GNP A 500

Chain	Residue
A	SER16
A	GLY40
A	ALA41
A	THR42
A	HIS127
A	LYS128
A	ASP130
A	ILE164
A	TRP165
A	GLY17
A	SER18
A	GLY19
A	LYS20
A	THR21
A	SER22
A	THR36
A	ARG37

Functional Information from PROSITE/UniProt

site_id	PS00214
Number of Residues	18
Details	FABP Cytosolic fatty-acid binding proteins signature. KAYkVnpDmNFEvFIHKV

Chain	Residue	Details
C	LYS163-VAL180

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	BINDING: BINDING => ECO:0000269\|PubMed:31601708, ECO:0000269\|PubMed:31601764, ECO:0000269\|PubMed:35338845, ECO:0000269\|PubMed:36697823, ECO:0007744\|PDB:6SB0, ECO:0007744\|PDB:6SB2, ECO:0007744\|PDB:6U62, ECO:0007744\|PDB:7T3C, ECO:0007744\|PDB:7UX2, ECO:0007744\|PDB:7UXC, ECO:0007744\|PDB:7UXH

Chain	Residue	Details
C	ARG71
A	GLY17
A	HIS127

site_id	SWS_FT_FI2
Number of Residues	1
Details	BINDING: BINDING => ECO:0000269\|PubMed:31601764, ECO:0000269\|PubMed:35338845, ECO:0007744\|PDB:6SB0, ECO:0007744\|PDB:6SB2, ECO:0007744\|PDB:7T3B, ECO:0007744\|PDB:7T3C

Chain	Residue	Details
C	SER72

site_id	SWS_FT_FI3
Number of Residues	1
Details	BINDING: BINDING => ECO:0000269\|PubMed:31601708, ECO:0000269\|PubMed:31601764, ECO:0000269\|PubMed:35338845, ECO:0000269\|PubMed:36697823, ECO:0007744\|PDB:6SB0, ECO:0007744\|PDB:6U62, ECO:0007744\|PDB:7T3B, ECO:0007744\|PDB:7UX2, ECO:0007744\|PDB:7UXC, ECO:0007744\|PDB:7UXH

Chain	Residue	Details
C	GLY73
A	THR21
A	THR36
A	ILE164

site_id	SWS_FT_FI4
Number of Residues	1
Details	BINDING: BINDING => ECO:0000269\|PubMed:32868926, ECO:0000269\|PubMed:36697823, ECO:0007744\|PDB:6WJ2, ECO:0007744\|PDB:6WJ3, ECO:0007744\|PDB:7UX2, ECO:0007744\|PDB:7UXC, ECO:0007744\|PDB:7UXH

Chain	Residue	Details
C	LYS74
A	THR42
N	LYS357

site_id	SWS_FT_FI5
Number of Residues	1
Details	BINDING: BINDING => ECO:0000269\|PubMed:31601708, ECO:0000269\|PubMed:31601764, ECO:0000269\|PubMed:32868926, ECO:0000269\|PubMed:35338845, ECO:0000269\|PubMed:36697823, ECO:0007744\|PDB:6SB0, ECO:0007744\|PDB:6SB2, ECO:0007744\|PDB:6U62, ECO:0007744\|PDB:6WJ2, ECO:0007744\|PDB:6WJ3, ECO:0007744\|PDB:7T3B, ECO:0007744\|PDB:7UX2, ECO:0007744\|PDB:7UXC, ECO:0007744\|PDB:7UXH

Chain	Residue	Details
C	ASN75
A	GLY65

site_id	SWS_FT_FI6
Number of Residues	1
Details	BINDING: BINDING => ECO:0000269\|PubMed:31601764, ECO:0000269\|PubMed:35338845, ECO:0000269\|PubMed:36697823, ECO:0007744\|PDB:6SB0, ECO:0007744\|PDB:6SB2, ECO:0007744\|PDB:7T3C, ECO:0007744\|PDB:7UX2, ECO:0007744\|PDB:7UXC, ECO:0007744\|PDB:7UXH

Chain	Residue	Details
C	SER76

site_id	SWS_FT_FI7
Number of Residues	3
Details	BINDING: BINDING => ECO:0000269\|PubMed:32868926, ECO:0007744\|PDB:6WJ2, ECO:0007744\|PDB:6WJ3

Chain	Residue	Details
C	THR90
C	THR96
C	ASP181

site_id	SWS_FT_FI8
Number of Residues	1
Details	BINDING: BINDING => ECO:0000269\|PubMed:35338845, ECO:0007744\|PDB:7T3B, ECO:0007744\|PDB:7T3C

Chain	Residue	Details
C	GLU94

site_id	SWS_FT_FI9
Number of Residues	1
Details	BINDING: BINDING => ECO:0000269\|PubMed:31601708, ECO:0000269\|PubMed:32868926, ECO:0000269\|PubMed:36697823, ECO:0007744\|PDB:6U62, ECO:0007744\|PDB:6WJ2, ECO:0007744\|PDB:6WJ3, ECO:0007744\|PDB:7UX2, ECO:0007744\|PDB:7UXC, ECO:0007744\|PDB:7UXH

Chain	Residue	Details
C	HIS178
A	LYS220
A	LYS230
A	LYS244

site_id	SWS_FT_FI10
Number of Residues	2
Details	BINDING: BINDING => ECO:0000269\|PubMed:31601708, ECO:0000269\|PubMed:35338845, ECO:0000269\|PubMed:36697823, ECO:0007744\|PDB:6U62, ECO:0007744\|PDB:7T3B, ECO:0007744\|PDB:7UX2, ECO:0007744\|PDB:7UXC, ECO:0007744\|PDB:7UXH

Chain	Residue	Details
C	LYS179
C	ILE220

site_id	SWS_FT_FI11
Number of Residues	1
Details	BINDING: BINDING => ECO:0000269\|PubMed:35338845, ECO:0000269\|PubMed:36697823, ECO:0007744\|PDB:7T3B, ECO:0007744\|PDB:7UX2, ECO:0007744\|PDB:7UXC, ECO:0007744\|PDB:7UXH

Chain	Residue	Details
C	SER219

site_id	SWS_FT_FI12
Number of Residues	1
Details	MOD_RES: Phosphoserine => ECO:0007744\|PubMed:20068231, ECO:0007744\|PubMed:23186163

Chain	Residue	Details
C	SER2

site_id	SWS_FT_FI13
Number of Residues	1
Details	MOD_RES: Phosphoserine => ECO:0007744\|PubMed:23186163

Chain	Residue	Details
C	SER15

site_id	SWS_FT_FI14
Number of Residues	1
Details	MOD_RES: Phosphothreonine => ECO:0000250\|UniProtKB:Q99K70

Chain	Residue	Details
C	THR96

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