5flc

Architecture of human mTOR Complex 1 - 5.9 Angstrom reconstruction

Method: ELECTRON MICROSCOPY Dmax: 270.5 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 × 12 PDB declaration: dodecameric(12) Consistent with protein copy count Chain B; UniProt 1382–2549 Chain F; UniProt 1382–2549 Fragment:FAT AND PIKK DOMAINS SERINE/THREONINE-PROTEIN KINASE MTOR × 2 SERINE/THREONINE-PROTEIN KINASE MTOR × 2 REGULATORY-ASSOCIATED PROTEIN OF MTOR × 2 FKBP × 2 TARGET OF RAPAMYCIN COMPLEX SUBUNIT LST8 × 2 (Q9BVC4) RAP RAPAMYCIN IMMUNOSUPPRESSANT DRUG × 2 ELECTRON MICROSCOPY cryo-EM buffer:100 MM NACL, 10 MM NABICINE, 1 MM TCEP;pH 8;100 MM NACL, 10 MM NABICINE, 1 MM TCEP cryo-EM vitrification conditions:Cryogen ETHANE;VITRIFICATION 1 -- CRYOGEN- ETHANE, HUMIDITY- 100, TEMPERATURE- 120, INSTRUMENT- FEI VITROBOT MARK I, METHOD- 4 SECOND BLOTTING, Resolution 5.90 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 4
Chains and sequence ranges Author chain B; PDBConstruct 1–1168; UniProt 1382–2549 Author chain F; PDBConstruct 1–1168; UniProt 1382–2549

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 × 12 PDB declaration: dodecameric(12) Consistent with protein copy count Chain D; UniProt 1–326 Chain H; UniProt 1–326 Not recorded SERINE/THREONINE-PROTEIN KINASE MTOR × 2 SERINE/THREONINE-PROTEIN KINASE MTOR × 2 REGULATORY-ASSOCIATED PROTEIN OF MTOR × 2 SERINE/THREONINE-PROTEIN KINASE MTOR × 2 (P42345) FKBP × 2 RAP RAPAMYCIN IMMUNOSUPPRESSANT DRUG × 2 ELECTRON MICROSCOPY cryo-EM buffer:100 MM NACL, 10 MM NABICINE, 1 MM TCEP;pH 8;100 MM NACL, 10 MM NABICINE, 1 MM TCEP cryo-EM vitrification conditions:Cryogen ETHANE;VITRIFICATION 1 -- CRYOGEN- ETHANE, HUMIDITY- 100, TEMPERATURE- 120, INSTRUMENT- FEI VITROBOT MARK I, METHOD- 4 SECOND BLOTTING, Resolution 5.90 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 6
Chains and sequence ranges Author chain D; PDBConstruct 1–326; UniProt 1–326 Author chain H; PDBConstruct 1–326; UniProt 1–326

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 5flc

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 5flc
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2. Structure Basics 2. Structure Basics

Entry ID entry_id5flc
Deposition date deposition_date2015-10-23
Structure title titleArchitecture of human mTOR Complex 1 - 5.9 Angstrom reconstruction
Keywords keywordsTRANSFERASE, RAPAMYCIN, MTORC1; TRANSFERASE
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier78.47
Radius of gyration Rg (electron density) rg_electron79.44
Forward intensity I(0) i05196700000.00
Molecular weight molecular_weight675300.0 kDa
Excluded volume excluded_volume874350 ų
Envelope volume envelope_volume1643600 ų
Hydration-shell volume shell_volume177270 ų
Envelope diameter envelope_diameter298.8
Shell Rg shell_rg77.66
Envelope Rg envelope_rg76.82
Shape Rg shape_rg79.40
Total Rg total_rg79.57
Total atoms total_atoms47528
Residues n_residues6966
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 dmax270.5
Rg (real space) rg_real81.28
Rg uncertainty (real space) rg_real_error1.61
I(0) (real space) i0_real5.1970e+09
I(0) uncertainty (real space) i0_real_error1.0260e+08
Rg (reciprocal space) rg_reciprocal78.37
I(0) (reciprocal space) i0_reciprocal5195000000.0000
Solution quality estimate total_estimate0.9190
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary94.7
Skewness Skewness skewness0.450
Kurtosis Kurtosis kurtosis0.020
Angular range angular_range— – 0.1000 −1
Current regularization parameter α current_alpha1.0400
Highest regularization parameter α highest_alpha353000000.0000
Real-space data points n_real_points21
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.895; Stabil: 0.894; Sysdev: 1.000; Positv: 1.000; Valcen: 0.982; Smooth: 0.726

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (7)

8. Citations (1)

9. Files and Curves (10)