3jbz

Crystal structure of mTOR docked into EM map of dimeric ATM kinase

Method: ELECTRON MICROSCOPY Dmax: 103.9 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 monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 1385–2549 Fragment:C-terminal domain (UNP RESIDUES 1385-2020, 2119-2549) ADP ADENOSINE-5'-DIPHOSPHATE × 1 MG MAGNESIUM ION × 2 MGF TRIFLUOROMAGNESATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:25 mM Tris pH 8.0, 100 mM NaCl, 1 mM TCEP, 10% glycerol;pH 8;25 mM Tris, 100 mM NaCl, 1 mM TCEP, 10% glycerol Resolution 28.00 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 1–1165; UniProt 1385–2549

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 3jbz

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 3jbz
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2. Structure Basics 2. Structure Basics

Entry ID entry_id3jbz
Deposition date deposition_date2015-11-03
Structure title titleCrystal structure of mTOR docked into EM map of dimeric ATM kinase
Keywords keywordsmTOR, PIKK, TRANSFERASE; TRANSFERASE
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier33.49
Radius of gyration Rg (electron density) rg_electron32.59
Forward intensity I(0) i0195137000.00
Molecular weight molecular_weight111270.0 kDa
Excluded volume excluded_volume139260 ų
Envelope volume envelope_volume184360 ų
Hydration-shell volume shell_volume46247 ų
Envelope diameter envelope_diameter103.8
Shell Rg shell_rg40.40
Envelope Rg envelope_rg32.13
Shape Rg shape_rg32.57
Total Rg total_rg33.31
Total atoms total_atoms7808
Residues n_residues960
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 dmax103.9
Rg (real space) rg_real33.35
Rg uncertainty (real space) rg_real_error0.54
I(0) (real space) i0_real1.9510e+08
I(0) uncertainty (real space) i0_real_error2.8240e+06
Rg (reciprocal space) rg_reciprocal33.44
I(0) (reciprocal space) i0_reciprocal195200000.0000
Solution quality estimate total_estimate0.9082
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary39.8
Skewness Skewness skewness0.123
Kurtosis Kurtosis kurtosis-0.606
Angular range angular_range— – 0.2350 −1
Current regularization parameter α current_alpha0.0001
Highest regularization parameter α highest_alpha34800000.0000
Real-space data points n_real_points48
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.951; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.998; Smooth: 0.950

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)