6cet

Cryo-EM structure of GATOR1

Method: ELECTRON MICROSCOPY Dmax: 166.3 Å Quality: REASONABLE

1. Protein Identity and Related Structures Protein Identity & Related Structures

GATOR complex protein NPRL2

Homo sapiens

UniProt Q8WTW4

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain N; UniProt 1–380 Not recorded GATOR complex protein NPRL3 × 1 (Q12980) GATOR complex protein DEPDC5 × 1 (O75140) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.40 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.

9 other PDB entries and 9 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name NPRL2_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain N; PDBConstruct 1–380; UniProt 1–380

GATOR complex protein NPRL3

Homo sapiens

UniProt Q12980

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain M; UniProt 1–569 Not recorded GATOR complex protein NPRL2 × 1 (Q8WTW4) GATOR complex protein DEPDC5 × 1 (O75140) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.40 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.

9 other PDB entries and 9 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name NPRL3_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain M; PDBConstruct 1–569; UniProt 1–569

GATOR complex protein DEPDC5

Homo sapiens

UniProt O75140

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain D; UniProt 1–1603 Not recorded GATOR complex protein NPRL2 × 1 (Q8WTW4) GATOR complex protein NPRL3 × 1 (Q12980) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.40 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.

10 other PDB entries and 10 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name DEPD5_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain D; PDBConstruct 1–1603; UniProt 1–1603

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 6cet

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6cet
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6cet
Deposition date deposition_date2018-02-12
Structure title titleCryo-EM structure of GATOR1
Keywords keywordsmTORC1 amino-acid sensing lysosome growth control, SIGNALING PROTEIN; SIGNALING PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier47.12
Radius of gyration Rg (electron density) rg_electron47.19
Forward intensity I(0) i0562481000.00
Molecular weight molecular_weight198940.0 kDa
Excluded volume excluded_volume250420 ų
Envelope volume envelope_volume387900 ų
Hydration-shell volume shell_volume69915 ų
Envelope diameter envelope_diameter178.6
Shell Rg shell_rg49.95
Envelope Rg envelope_rg46.54
Shape Rg shape_rg47.17
Total Rg total_rg47.39
Total atoms total_atoms14012
Residues n_residues1741
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 dmax166.3
Rg (real space) rg_real47.34
Rg uncertainty (real space) rg_real_error1.74
I(0) (real space) i0_real5.6250e+08
I(0) uncertainty (real space) i0_real_error1.0990e+07
Rg (reciprocal space) rg_reciprocal47.13
I(0) (reciprocal space) i0_reciprocal562300000.0000
Solution quality estimate total_estimate0.6304
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary55.4
Skewness Skewness skewness0.472
Kurtosis Kurtosis kurtosis-0.119
Angular range angular_range— – 0.1650 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha51540000.0000
Real-space data points n_real_points34
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.789; Stabil: 1.000; Sysdev: 0.006; Positv: 1.000; Valcen: 0.987; Smooth: 0.820

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)