7owg

human DEPTOR in a complex with mutant human mTORC1 A1459P

Method: ELECTRON MICROSCOPY Dmax: 224.6 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 B; UniProt 1–16 Chain B; UniProt 31–36 Chain B; UniProt 54–355 Chain B; UniProt 379–2549 Mutation:A1459P Target of rapamycin complex subunit LST8 × 2 (Q9BVC4) DEP domain-containing mTOR-interacting protein × 2 (Q8TB45) Regulatory-associated protein of mTOR × 2 (Q8N122) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;50 mM HEPES, pH 7.5, 200 mM NaCl, 1 mM TCEP, 1 mM MgCl2, 500 uM AMP-PNP cryo-EM vitrification conditions:Cryogen ETHANE;blotting time of 2 s and a force of -15. Resolution 4.70 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 1–16; UniProt 1–16 Author chain B; PDBConstruct 31–36; UniProt 31–36 Author chain B; PDBConstruct 54–355; UniProt 54–355 Author chain B; PDBConstruct 379–2549; UniProt 379–2549

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 E; UniProt 1–326 Not recorded Serine/threonine-protein kinase mTOR × 2 (P42345) DEP domain-containing mTOR-interacting protein × 2 (Q8TB45) Regulatory-associated protein of mTOR × 2 (Q8N122) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;50 mM HEPES, pH 7.5, 200 mM NaCl, 1 mM TCEP, 1 mM MgCl2, 500 uM AMP-PNP cryo-EM vitrification conditions:Cryogen ETHANE;blotting time of 2 s and a force of -15. Resolution 4.70 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

DEP domain-containing mTOR-interacting protein

Homo sapiens

UniProt Q8TB45

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 O; UniProt 1–409 Not recorded Serine/threonine-protein kinase mTOR × 2 (P42345) Target of rapamycin complex subunit LST8 × 2 (Q9BVC4) Regulatory-associated protein of mTOR × 2 (Q8N122) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;50 mM HEPES, pH 7.5, 200 mM NaCl, 1 mM TCEP, 1 mM MgCl2, 500 uM AMP-PNP cryo-EM vitrification conditions:Cryogen ETHANE;blotting time of 2 s and a force of -15. Resolution 4.70 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.

8 other PDB entries and 8 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name DPTOR_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain O; PDBConstruct 1–409; UniProt 1–409

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 Y; UniProt 1–1335 Not recorded Serine/threonine-protein kinase mTOR × 2 (P42345) Target of rapamycin complex subunit LST8 × 2 (Q9BVC4) DEP domain-containing mTOR-interacting protein × 2 (Q8TB45) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;50 mM HEPES, pH 7.5, 200 mM NaCl, 1 mM TCEP, 1 mM MgCl2, 500 uM AMP-PNP cryo-EM vitrification conditions:Cryogen ETHANE;blotting time of 2 s and a force of -15. Resolution 4.70 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 4
Chains and sequence ranges Author chain Y; PDBConstruct 1–1335; UniProt 1–1335

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 7owg

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7owg
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7owg
Deposition date deposition_date2021-06-18
Structure title titlehuman DEPTOR in a complex with mutant human mTORC1 A1459P
Keywords keywords;kinase, PIKK, mTOR, cancer-associated mutation, DEPTOR, partial inhibitor, cancer, PDZ, non-canonical PDZ binding, SIGNALING PROTEIN ;; SIGNALING PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier73.54
Radius of gyration Rg (electron density) rg_electron73.97
Forward intensity I(0) i02263950000.00
Molecular weight molecular_weight405980.0 kDa
Excluded volume excluded_volume510390 ų
Envelope volume envelope_volume841940 ų
Hydration-shell volume shell_volume104280 ų
Envelope diameter envelope_diameter252.8
Shell Rg shell_rg63.23
Envelope Rg envelope_rg72.06
Shape Rg shape_rg73.98
Total Rg total_rg73.71
Total atoms total_atoms57277
Residues n_residues3594
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 dmax224.6
Rg (real space) rg_real73.80
Rg uncertainty (real space) rg_real_error1.63
I(0) (real space) i0_real2.2610e+09
I(0) uncertainty (real space) i0_real_error5.0540e+07
Rg (reciprocal space) rg_reciprocal71.50
I(0) (reciprocal space) i0_reciprocal2252000000.0000
Solution quality estimate total_estimate0.8276
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary64.2
Skewness Skewness skewness0.528
Kurtosis Kurtosis kurtosis-0.427
Angular range angular_range— – 0.1050 −1
Current regularization parameter α current_alpha0.0054
Highest regularization parameter α highest_alpha113800000.0000
Real-space data points n_real_points22
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.914; Stabil: 0.997; Sysdev: 1.000; Positv: 1.000; Valcen: 0.992; Smooth: 0.027

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)