9f45

cryo-EM structure of human LST2 bound to human mTOR complex 1

Method: ELECTRON MICROSCOPY Dmax: 275.1 Å Quality: EXCELLENT

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 × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain A; UniProt 1–2549 Chain B; UniProt 1–2549 Not recorded Target of rapamycin complex subunit LST8 × 2 (Q9BVC4) Regulatory-associated protein of mTOR × 2 (Q8N122) Lateral signaling target protein 2 homolog × 2 (Q9HCC9) IHP INOSITOL HEXAKISPHOSPHATE × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.74 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 1–2549; UniProt 1–2549 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 × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain C; UniProt 1–326 Chain D; UniProt 1–326 Not recorded Serine/threonine-protein kinase mTOR × 2 (P42345) Regulatory-associated protein of mTOR × 2 (Q8N122) Lateral signaling target protein 2 homolog × 2 (Q9HCC9) IHP INOSITOL HEXAKISPHOSPHATE × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.74 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 C; PDBConstruct 1–326; UniProt 1–326 Author chain D; 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 × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain E; UniProt 1–1335 Chain F; UniProt 1–1335 Not recorded Serine/threonine-protein kinase mTOR × 2 (P42345) Target of rapamycin complex subunit LST8 × 2 (Q9BVC4) Lateral signaling target protein 2 homolog × 2 (Q9HCC9) IHP INOSITOL HEXAKISPHOSPHATE × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.74 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 E; PDBConstruct 29–1363; UniProt 1–1335 Author chain F; PDBConstruct 29–1363; UniProt 1–1335

Lateral signaling target protein 2 homolog

Homo sapiens

UniProt Q9HCC9

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 × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain G; UniProt 1–887 Chain H; UniProt 1–887 Not recorded Serine/threonine-protein kinase mTOR × 2 (P42345) Target of rapamycin complex subunit LST8 × 2 (Q9BVC4) Regulatory-associated protein of mTOR × 2 (Q8N122) IHP INOSITOL HEXAKISPHOSPHATE × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.74 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 3 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name LST2_HUMAN
Isoform
PDB entities 4
Chains and sequence ranges Author chain G; PDBConstruct 1–887; UniProt 1–887 Author chain H; PDBConstruct 1–887; UniProt 1–887

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 9f45

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9f45
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9f45
Deposition date deposition_date2024-04-26
Structure title titlecryo-EM structure of human LST2 bound to human mTOR complex 1
Keywords keywordsMTOR, MTORC1, LST2, ZFYVE28, EGFR, TOS, SIGNALING PROTEIN; SIGNALING PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier79.36
Radius of gyration Rg (electron density) rg_electron79.00
Forward intensity I(0) i08882890000.00
Molecular weight molecular_weight808990.0 kDa
Excluded volume excluded_volume1016100 ų
Envelope volume envelope_volume1682700 ų
Hydration-shell volume shell_volume182110 ų
Envelope diameter envelope_diameter297.8
Shell Rg shell_rg77.70
Envelope Rg envelope_rg76.33
Shape Rg shape_rg79.03
Total Rg total_rg78.88
Total atoms total_atoms56848
Residues n_residues7140
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 dmax275.1
Rg (real space) rg_real82.73
Rg uncertainty (real space) rg_real_error1.44
I(0) (real space) i0_real8.8910e+09
I(0) uncertainty (real space) i0_real_error1.4560e+08
Rg (reciprocal space) rg_reciprocal79.08
I(0) (reciprocal space) i0_reciprocal8876000000.0000
Solution quality estimate total_estimate0.9123
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary96.3
Skewness Skewness skewness0.517
Kurtosis Kurtosis kurtosis0.093
Angular range angular_range— – 0.1000 −1
Current regularization parameter α current_alpha1.1520
Highest regularization parameter α highest_alpha405800000.0000
Real-space data points n_real_points21
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.870; Stabil: 0.875; Sysdev: 1.000; Positv: 1.000; Valcen: 0.980; Smooth: 0.669

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

8. Citations (1)

9. Files and Curves (10)