6bcu

Cryo-EM structure of the activated RHEB-mTORC1 refined to 3.4 angstrom

Method: ELECTRON MICROSCOPY Dmax: 264.6 Å Quality: EXCELLENT

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

Serine/threonine-protein kinase 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 × 10 PDB declaration: decameric(10) Consistent with protein copy count Chain A; UniProt 579–2549 Chain B; UniProt 579–2549 Not recorded Target of rapamycin complex subunit LST8 × 2 (Q9BVC4) Regulatory-associated protein of mTOR,Regulatory-associated protein of mTOR × 2 (Q8N122) Eukaryotic translation initiation factor 4E-binding protein 1 × 2 (Q13541) GTP-binding protein Rheb × 2 (Q15382) ATP ADENOSINE-5'-TRIPHOSPHATE × 2 MG MAGNESIUM ION × 6 GTP GUANOSINE-5'-TRIPHOSPHATE × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.80 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 579–2549; UniProt 579–2549 Author chain B; PDBConstruct 579–2549; UniProt 579–2549

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 × 10 PDB declaration: decameric(10) Consistent with protein copy count Chain D; UniProt 1–326 Chain E; UniProt 1–326 Not recorded Serine/threonine-protein kinase mTOR,Serine/threonine-protein kinase mTOR × 2 (P42345) Regulatory-associated protein of mTOR,Regulatory-associated protein of mTOR × 2 (Q8N122) Eukaryotic translation initiation factor 4E-binding protein 1 × 2 (Q13541) GTP-binding protein Rheb × 2 (Q15382) ATP ADENOSINE-5'-TRIPHOSPHATE × 2 MG MAGNESIUM ION × 6 GTP GUANOSINE-5'-TRIPHOSPHATE × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.80 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 D; PDBConstruct 1–326; UniProt 1–326 Author chain E; PDBConstruct 1–326; UniProt 1–326

Regulatory-associated protein of mTOR,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 × 10 PDB declaration: decameric(10) Consistent with protein copy count Chain W; UniProt 2–661 Chain W; UniProt 504–1177 Chain Y; UniProt 2–661 Chain Y; UniProt 504–1177 Not recorded Serine/threonine-protein kinase mTOR,Serine/threonine-protein kinase mTOR × 2 (P42345) Target of rapamycin complex subunit LST8 × 2 (Q9BVC4) Eukaryotic translation initiation factor 4E-binding protein 1 × 2 (Q13541) GTP-binding protein Rheb × 2 (Q15382) ATP ADENOSINE-5'-TRIPHOSPHATE × 2 MG MAGNESIUM ION × 6 GTP GUANOSINE-5'-TRIPHOSPHATE × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.80 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 3
Chains and sequence ranges Author chain W; PDBConstruct 10–669; UniProt 2–661 Author chain W; PDBConstruct 670–1343; UniProt 504–1177 Author chain Y; PDBConstruct 10–669; UniProt 2–661 Author chain Y; PDBConstruct 670–1343; UniProt 504–1177

Eukaryotic translation initiation factor 4E-binding protein 1

Homo sapiens

UniProt Q13541

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 × 10 PDB declaration: decameric(10) Consistent with protein copy count Chain X; UniProt 1–118 Chain Z; UniProt 1–118 Not recorded Serine/threonine-protein kinase mTOR,Serine/threonine-protein kinase mTOR × 2 (P42345) Target of rapamycin complex subunit LST8 × 2 (Q9BVC4) Regulatory-associated protein of mTOR,Regulatory-associated protein of mTOR × 2 (Q8N122) GTP-binding protein Rheb × 2 (Q15382) ATP ADENOSINE-5'-TRIPHOSPHATE × 2 MG MAGNESIUM ION × 6 GTP GUANOSINE-5'-TRIPHOSPHATE × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.80 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 29 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name 4EBP1_HUMAN
Isoform
PDB entities 4
Chains and sequence ranges Author chain X; PDBConstruct 5–122; UniProt 1–118 Author chain Z; PDBConstruct 5–122; UniProt 1–118

GTP-binding protein Rheb

Homo sapiens

UniProt Q15382

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 × 10 PDB declaration: decameric(10) Consistent with protein copy count Chain R; UniProt 1–184 Chain S; UniProt 1–184 Not recorded Serine/threonine-protein kinase mTOR,Serine/threonine-protein kinase mTOR × 2 (P42345) Target of rapamycin complex subunit LST8 × 2 (Q9BVC4) Regulatory-associated protein of mTOR,Regulatory-associated protein of mTOR × 2 (Q8N122) Eukaryotic translation initiation factor 4E-binding protein 1 × 2 (Q13541) ATP ADENOSINE-5'-TRIPHOSPHATE × 2 MG MAGNESIUM ION × 6 GTP GUANOSINE-5'-TRIPHOSPHATE × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.80 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.

14 other PDB entries and 29 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RHEB_HUMAN
Isoform
PDB entities 5
Chains and sequence ranges Author chain R; PDBConstruct 5–188; UniProt 1–184 Author chain S; PDBConstruct 5–188; UniProt 1–184

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 6bcu

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id6bcu
Deposition date deposition_date2017-10-20
Structure title titleCryo-EM structure of the activated RHEB-mTORC1 refined to 3.4 angstrom
Keywords keywordsPIKK, TRANSFERASE; TRANSFERASE
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier76.78
Radius of gyration Rg (electron density) rg_electron76.19
Forward intensity I(0) i09792750000.00
Molecular weight molecular_weight849000.0 kDa
Excluded volume excluded_volume1066200 ų
Envelope volume envelope_volume1719800 ų
Hydration-shell volume shell_volume189470 ų
Envelope diameter envelope_diameter280.9
Shell Rg shell_rg77.24
Envelope Rg envelope_rg74.02
Shape Rg shape_rg76.21
Total Rg total_rg76.12
Total atoms total_atoms119740
Residues n_residues7494
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 dmax264.6
Rg (real space) rg_real79.44
Rg uncertainty (real space) rg_real_error1.60
I(0) (real space) i0_real9.7930e+09
I(0) uncertainty (real space) i0_real_error1.9810e+08
Rg (reciprocal space) rg_reciprocal76.92
I(0) (reciprocal space) i0_reciprocal9796000000.0000
Solution quality estimate total_estimate0.9104
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary92.6
Skewness Skewness skewness0.475
Kurtosis Kurtosis kurtosis0.101
Angular range angular_range— – 0.1000 −1
Current regularization parameter α current_alpha0.9817
Highest regularization parameter α highest_alpha435800000.0000
Real-space data points n_real_points21
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.850; Stabil: 0.910; Sysdev: 1.000; Positv: 1.000; Valcen: 0.966; Smooth: 0.745

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (8)

8. Citations (1)

9. Files and Curves (10)