8rck

CryoEM structure of mTORC1 with a paediatric kidney cancer-associated 1455-EWED-1458 duplication in mTOR, Focused on one protomer copy.

Method: ELECTRON MICROSCOPY Dmax: 213.5 Å Quality: GOOD

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

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain B; UniProt 1–2549 Not recorded Target of rapamycin complex subunit LST8 × 1 (Q9BVC4) Regulatory-associated protein of mTOR × 1 (Q8N122) Eukaryotic translation initiation factor 4E-binding protein 1 × 1 (Q13541) ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 1 MG MAGNESIUM ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.40 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 B; PDBConstruct 1–2549; UniProt 1–2549

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain E; UniProt 1–326 Not recorded Serine/threonine-protein kinase mTOR × 1 (P42345) Regulatory-associated protein of mTOR × 1 (Q8N122) Eukaryotic translation initiation factor 4E-binding protein 1 × 1 (Q13541) ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 1 MG MAGNESIUM ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.40 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

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain Y; UniProt 1–1335 Not recorded Serine/threonine-protein kinase mTOR × 1 (P42345) Target of rapamycin complex subunit LST8 × 1 (Q9BVC4) Eukaryotic translation initiation factor 4E-binding protein 1 × 1 (Q13541) ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 1 MG MAGNESIUM ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.40 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 Y; PDBConstruct 1–1335; UniProt 1–1335

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain X; UniProt 1–118 Not recorded Serine/threonine-protein kinase mTOR × 1 (P42345) Target of rapamycin complex subunit LST8 × 1 (Q9BVC4) Regulatory-associated protein of mTOR × 1 (Q8N122) ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 1 MG MAGNESIUM ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.40 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 1–118; UniProt 1–118

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 8rck

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8rck
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8rck
Deposition date deposition_date2023-12-06
最后修订 last_revision2024-09-11
Structure title titleCryoEM structure of mTORC1 with a paediatric kidney cancer-associated 1455-EWED-1458 duplication in mTOR, Focused on one protomer copy.
Keywords keywordsTarget of Rapamycin, mTOR, Cancer-associated mutants, SIGNALING PROTEIN; SIGNALING PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier71.73
Radius of gyration Rg (electron density) rg_electron72.03
Forward intensity I(0) i02067060000.00
Molecular weight molecular_weight387800.0 kDa
Excluded volume excluded_volume487770 ų
Envelope volume envelope_volume809500 ų
Hydration-shell volume shell_volume102920 ų
Envelope diameter envelope_diameter244.9
Shell Rg shell_rg62.17
Envelope Rg envelope_rg69.74
Shape Rg shape_rg72.04
Total Rg total_rg71.75
Total atoms total_atoms54652
Residues n_residues3405
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 dmax213.5
Rg (real space) rg_real71.82
Rg uncertainty (real space) rg_real_error1.41
I(0) (real space) i0_real2.0630e+09
I(0) uncertainty (real space) i0_real_error4.3770e+07
Rg (reciprocal space) rg_reciprocal70.11
I(0) (reciprocal space) i0_reciprocal2059000000.0000
Solution quality estimate total_estimate0.8372
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary67.9
Skewness Skewness skewness0.484
Kurtosis Kurtosis kurtosis-0.473
Angular range angular_range— – 0.1100 −1
Current regularization parameter α current_alpha0.0088
Highest regularization parameter α highest_alpha96130000.0000
Real-space data points n_real_points23
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.955; Stabil: 0.998; Sysdev: 1.000; Positv: 1.000; Valcen: 0.991; Smooth: 0.026

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

8. Citations (1)

9. Files and Curves (10)