9tds

cryo-EM structure of dephosphorylated mTOR complex 2, overall refinement

Method: ELECTRON MICROSCOPY Dmax: 274.3 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 × 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) Rapamycin-insensitive companion of mTOR × 2 (Q6R327) Target of rapamycin complex 2 subunit MAPKAP1 × 2 (Q9BPZ7) IHP INOSITOL HEXAKISPHOSPHATE × 2 ZN ZINC ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.30 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 42–2590; UniProt 1–2549 Author chain B; PDBConstruct 42–2590; 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) Rapamycin-insensitive companion of mTOR × 2 (Q6R327) Target of rapamycin complex 2 subunit MAPKAP1 × 2 (Q9BPZ7) IHP INOSITOL HEXAKISPHOSPHATE × 2 ZN ZINC ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.30 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

Rapamycin-insensitive companion of mTOR

Homo sapiens

UniProt Q6R327

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 1–1708 Chain F; UniProt 1–1708 Not recorded Serine/threonine-protein kinase mTOR × 2 (P42345) Target of rapamycin complex subunit LST8 × 2 (Q9BVC4) Target of rapamycin complex 2 subunit MAPKAP1 × 2 (Q9BPZ7) IHP INOSITOL HEXAKISPHOSPHATE × 2 ZN ZINC ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.30 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.

15 other PDB entries and 15 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RICTR_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain E; PDBConstruct 27–1734; UniProt 1–1708 Author chain F; PDBConstruct 27–1734; UniProt 1–1708

Target of rapamycin complex 2 subunit MAPKAP1

Homo sapiens

UniProt Q9BPZ7

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 2–522 Chain H; UniProt 2–522 Non-standard monomer:Yes (specific site not provided by mmCIF) Serine/threonine-protein kinase mTOR × 2 (P42345) Target of rapamycin complex subunit LST8 × 2 (Q9BVC4) Rapamycin-insensitive companion of mTOR × 2 (Q6R327) IHP INOSITOL HEXAKISPHOSPHATE × 2 ZN ZINC ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.30 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.

22 other PDB entries and 24 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SIN1_HUMAN
Isoform
PDB entities 4
Chains and sequence ranges Author chain G; PDBConstruct 2–522; UniProt 2–522 Author chain H; PDBConstruct 2–522; UniProt 2–522

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 9tds

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id9tds
Deposition date deposition_date2025-11-24
Structure title titlecryo-EM structure of dephosphorylated mTOR complex 2, overall refinement
Keywords keywordsKinase, Complex, Signaling protein, TRANSFERASE; TRANSFERASE
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier74.20
Radius of gyration Rg (electron density) rg_electron73.85
Forward intensity I(0) i07717910000.00
Molecular weight molecular_weight752350.0 kDa
Excluded volume excluded_volume945430 ų
Envelope volume envelope_volume1549100 ų
Hydration-shell volume shell_volume175960 ų
Envelope diameter envelope_diameter245.4
Shell Rg shell_rg74.15
Envelope Rg envelope_rg70.74
Shape Rg shape_rg73.85
Total Rg total_rg73.86
Total atoms total_atoms52832
Residues n_residues6562
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 dmax274.3
Rg (real space) rg_real78.09
Rg uncertainty (real space) rg_real_error1.78
I(0) (real space) i0_real7.7710e+09
I(0) uncertainty (real space) i0_real_error1.6270e+08
Rg (reciprocal space) rg_reciprocal74.51
I(0) (reciprocal space) i0_reciprocal7724000000.0000
Solution quality estimate total_estimate0.8942
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary91.4
Skewness Skewness skewness0.532
Kurtosis Kurtosis kurtosis0.233
Angular range angular_range— – 0.1050 −1
Current regularization parameter α current_alpha0.8738
Highest regularization parameter α highest_alpha377600000.0000
Real-space data points n_real_points22
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.776; Stabil: 0.868; Sysdev: 1.000; Positv: 1.000; Valcen: 0.975; Smooth: 0.817

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

8. Citations (1)

9. Files and Curves (10)