9dx2

Human GATOR2 complex - CASTOR1 bound state

Method: ELECTRON MICROSCOPY Dmax: 276.2 Å Quality: GOOD

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

Cytosolic arginine sensor for mTORC1 subunit 1

Homo sapiens

UniProt Q8WTX7

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 1–328 Chain F; UniProt 1–328 Chain G; UniProt 1–328 Not recorded GATOR2 complex protein MIOS × 2 Nucleoporin SEH1 × 1 Protein SEC13 homolog × 1 GATOR2 complex protein WDR24 × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.40 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 14 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CAST1_HUMAN
Isoform
PDB entities 4
Chains and sequence ranges Author chain E; PDBConstruct 1–328; UniProt 1–328 Author chain F; PDBConstruct 1–328; UniProt 1–328 Author chain G; PDBConstruct 1–328; UniProt 1–328

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 9dx2

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9dx2
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9dx2
Deposition date deposition_date2024-10-10
Structure title titleHuman GATOR2 complex - CASTOR1 bound state
Keywords keywordsSignaling protein, nutrient sensor, mTORC1 pathway, stress-responsive protein; SIGNALING PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier79.08
Radius of gyration Rg (electron density) rg_electron78.99
Forward intensity I(0) i03352700000.00
Molecular weight molecular_weight485960.0 kDa
Excluded volume excluded_volume604830 ų
Envelope volume envelope_volume1171400 ų
Hydration-shell volume shell_volume124360 ų
Envelope diameter envelope_diameter241.7
Shell Rg shell_rg79.92
Envelope Rg envelope_rg75.27
Shape Rg shape_rg79.05
Total Rg total_rg78.77
Total atoms total_atoms34252
Residues n_residues4631
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 dmax276.2
Rg (real space) rg_real79.09
Rg uncertainty (real space) rg_real_error2.42
I(0) (real space) i0_real3.3540e+09
I(0) uncertainty (real space) i0_real_error7.6550e+07
Rg (reciprocal space) rg_reciprocal79.60
I(0) (reciprocal space) i0_reciprocal3357000000.0000
Solution quality estimate total_estimate0.7839
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary110.5
Skewness Skewness skewness0.030
Kurtosis Kurtosis kurtosis-0.613
Angular range angular_range— – 0.1000 −1
Current regularization parameter α current_alpha0.0679
Highest regularization parameter α highest_alpha80370000.0000
Real-space data points n_real_points21
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.730; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.995; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

8. Citations (1)

9. Files and Curves (10)