6sb0

cryo-EM structure of mTORC1 bound to PRAS40-fused active RagA/C GTPases

Method: ELECTRON MICROSCOPY Dmax: 240.2 Å Quality: EXCELLENT

1. Protein Identity and Related Structures Protein Identity & Related Structures

mTOR,Serine/threonine-protein kinase mTOR,mTOR,Serine/threonine-protein kinase mTOR

Homo sapiens

UniProt P42345

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 12 PDB declaration: dodecameric(12) Consistent with protein copy count Chain A; UniProt 60–355 Chain A; UniProt 381–2549 Chain B; UniProt 60–355 Chain B; UniProt 381–2549 Not recorded Target of rapamycin complex subunit LST8 × 2 (Q9BVC4) Ras-related GTP-binding protein A × 2 (Q7L523) Ras-related GTP-binding protein C × 2 (Q9HB90) Regulatory-associated protein of mTOR × 2 (Q8N122) Proline-rich AKT1 substrate 1 × 2 (Q96B36) GTP GUANOSINE-5'-TRIPHOSPHATE × 2 GDP GUANOSINE-5'-DIPHOSPHATE × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7;50mM HEPES pH 7.0, 100mM NaCl, 2mM MgCl2, 1mM TCEP cryo-EM vitrification conditions:Cryogen ETHANE Resolution 5.50 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

66 other PDB entries and 84 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name MTOR_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 60–355; UniProt 60–355 Author chain A; PDBConstruct 381–2549; UniProt 381–2549 Author chain B; PDBConstruct 60–355; UniProt 60–355 Author chain B; PDBConstruct 381–2549; UniProt 381–2549

Target of rapamycin complex subunit LST8

Homo sapiens

UniProt Q9BVC4

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 12 PDB declaration: dodecameric(12) Consistent with protein copy count Chain E; UniProt 1–326 Chain H; UniProt 1–326 Not recorded mTOR,Serine/threonine-protein kinase mTOR,mTOR,Serine/threonine-protein kinase mTOR × 2 (P42345) Ras-related GTP-binding protein A × 2 (Q7L523) Ras-related GTP-binding protein C × 2 (Q9HB90) Regulatory-associated protein of mTOR × 2 (Q8N122) Proline-rich AKT1 substrate 1 × 2 (Q96B36) GTP GUANOSINE-5'-TRIPHOSPHATE × 2 GDP GUANOSINE-5'-DIPHOSPHATE × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7;50mM HEPES pH 7.0, 100mM NaCl, 2mM MgCl2, 1mM TCEP cryo-EM vitrification conditions:Cryogen ETHANE Resolution 5.50 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

44 other PDB entries and 52 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name LST8_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain E; PDBConstruct 1–326; UniProt 1–326 Author chain H; PDBConstruct 1–326; UniProt 1–326

Ras-related GTP-binding protein A

Homo sapiens

UniProt Q7L523

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 12 PDB declaration: dodecameric(12) Consistent with protein copy count Chain C; UniProt 1–313 Chain I; UniProt 1–313 Mutation:Q66L mTOR,Serine/threonine-protein kinase mTOR,mTOR,Serine/threonine-protein kinase mTOR × 2 (P42345) Target of rapamycin complex subunit LST8 × 2 (Q9BVC4) Ras-related GTP-binding protein C × 2 (Q9HB90) Regulatory-associated protein of mTOR × 2 (Q8N122) Proline-rich AKT1 substrate 1 × 2 (Q96B36) GTP GUANOSINE-5'-TRIPHOSPHATE × 2 GDP GUANOSINE-5'-DIPHOSPHATE × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7;50mM HEPES pH 7.0, 100mM NaCl, 2mM MgCl2, 1mM TCEP cryo-EM vitrification conditions:Cryogen ETHANE Resolution 5.50 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

20 other PDB entries and 22 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RRAGA_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 1–313; UniProt 1–313 Author chain I; PDBConstruct 1–313; UniProt 1–313

Ras-related GTP-binding protein C

Homo sapiens

UniProt Q9HB90

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 12 PDB declaration: dodecameric(12) Consistent with protein copy count Chain D; UniProt 1–399 Chain J; UniProt 1–399 Mutation:T90N mTOR,Serine/threonine-protein kinase mTOR,mTOR,Serine/threonine-protein kinase mTOR × 2 (P42345) Target of rapamycin complex subunit LST8 × 2 (Q9BVC4) Ras-related GTP-binding protein A × 2 (Q7L523) Regulatory-associated protein of mTOR × 2 (Q8N122) Proline-rich AKT1 substrate 1 × 2 (Q96B36) GTP GUANOSINE-5'-TRIPHOSPHATE × 2 GDP GUANOSINE-5'-DIPHOSPHATE × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7;50mM HEPES pH 7.0, 100mM NaCl, 2mM MgCl2, 1mM TCEP cryo-EM vitrification conditions:Cryogen ETHANE Resolution 5.50 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

20 other PDB entries and 22 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RRAGC_HUMAN
Isoform
PDB entities 4
Chains and sequence ranges Author chain D; PDBConstruct 1–399; UniProt 1–399 Author chain J; PDBConstruct 1–399; UniProt 1–399

Regulatory-associated protein of mTOR

Homo sapiens

UniProt Q8N122

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 12 PDB declaration: dodecameric(12) Consistent with protein copy count Chain N; UniProt 1–1335 Chain Y; UniProt 1–1335 Not recorded mTOR,Serine/threonine-protein kinase mTOR,mTOR,Serine/threonine-protein kinase mTOR × 2 (P42345) Target of rapamycin complex subunit LST8 × 2 (Q9BVC4) Ras-related GTP-binding protein A × 2 (Q7L523) Ras-related GTP-binding protein C × 2 (Q9HB90) Proline-rich AKT1 substrate 1 × 2 (Q96B36) GTP GUANOSINE-5'-TRIPHOSPHATE × 2 GDP GUANOSINE-5'-DIPHOSPHATE × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7;50mM HEPES pH 7.0, 100mM NaCl, 2mM MgCl2, 1mM TCEP cryo-EM vitrification conditions:Cryogen ETHANE Resolution 5.50 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

21 other PDB entries and 21 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RPTOR_HUMAN
Isoform
PDB entities 5
Chains and sequence ranges Author chain N; PDBConstruct 1–1335; UniProt 1–1335 Author chain Y; PDBConstruct 1–1335; UniProt 1–1335

Proline-rich AKT1 substrate 1

Homo sapiens

UniProt Q96B36

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 12 PDB declaration: dodecameric(12) Consistent with protein copy count Chain O; UniProt 21–276 Chain T; UniProt 21–276 Not recorded mTOR,Serine/threonine-protein kinase mTOR,mTOR,Serine/threonine-protein kinase mTOR × 2 (P42345) Target of rapamycin complex subunit LST8 × 2 (Q9BVC4) Ras-related GTP-binding protein A × 2 (Q7L523) Ras-related GTP-binding protein C × 2 (Q9HB90) Regulatory-associated protein of mTOR × 2 (Q8N122) GTP GUANOSINE-5'-TRIPHOSPHATE × 2 GDP GUANOSINE-5'-DIPHOSPHATE × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7;50mM HEPES pH 7.0, 100mM NaCl, 2mM MgCl2, 1mM TCEP cryo-EM vitrification conditions:Cryogen ETHANE Resolution 5.50 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

3 other PDB entries and 5 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name AKTS1_HUMAN
Isoform Q96B36-3
PDB entities 6
Chains and sequence ranges Author chain O; PDBConstruct 1–256; UniProt 21–276 Author chain T; PDBConstruct 1–256; UniProt 21–276

The page prioritizes protein identity, the current assembly, associated components, oligomeric state and cross-PDB links. Chain mapping and sequence ranges are retained as data evidence. Internal IDs, import timestamps and assembly operation expressions are maintenance fields and are not shown here.

SAXS scattering curve SAXS Profile

SAXS profile for 6sb0

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6sb0
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6sb0
Deposition date deposition_date2019-07-18
Structure title titlecryo-EM structure of mTORC1 bound to PRAS40-fused active RagA/C GTPases
Keywords keywordssmall GTPases, mTORC1 activator, roadblock domain, GTPase domain, SIGNALING PROTEIN; SIGNALING PROTEIN
Experimental Method methodELECTRON MICROSCOPY

3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier88.13
Radius of gyration Rg (electron density) rg_electron88.79
Forward intensity I(0) i06949200000.00
Molecular weight molecular_weight577960.0 kDa
Excluded volume excluded_volume665430 ų
Envelope volume envelope_volume1725300 ų
Hydration-shell volume shell_volume175280 ų
Envelope diameter envelope_diameter336.7
Shell Rg shell_rg78.78
Envelope Rg envelope_rg84.85
Shape Rg shape_rg88.78
Total Rg total_rg88.69
Total atoms total_atoms41284
Residues n_residues8305
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 −1
Data points n_points101
Shell type shell_typedirectional
Solvent electron density solvent_density0.3340 e/ų
Shell contrast contrast_shell0.0300 e/ų
CRYSOL version crysol_version4.1.3

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax240.2
Rg (real space) rg_real82.66
Rg uncertainty (real space) rg_real_error1.06
I(0) (real space) i0_real6.6380e+09
I(0) uncertainty (real space) i0_real_error1.2080e+08
Rg (reciprocal space) rg_reciprocal86.07
I(0) (reciprocal space) i0_reciprocal6906000000.0000
Solution quality estimate total_estimate0.9189
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary106.8
Skewness Skewness skewness0.203
Kurtosis Kurtosis kurtosis-0.517
Angular range angular_range— – 0.0900 −1
Current regularization parameter α current_alpha0.6271
Highest regularization parameter α highest_alpha340500000.0000
Real-space data points n_real_points19
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.001; Oscil: 0.998; Stabil: 0.985; Sysdev: 1.000; Positv: 1.000; Valcen: 0.997; Smooth: 0.001

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (8)

8. Citations (1)

9. Files and Curves (10)