9v0j

Cryo-EM structure of GATOR1-KICSTOR complex

Method: ELECTRON MICROSCOPY Dmax: 183.5 Å Quality: GOOD

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

GATOR1 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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 1–380 Not recorded GATOR1 complex protein NPRL3 × 1 (Q12980) GATOR1 complex protein DEPDC5 × 1 (O75140) KICSTOR complex protein SZT2 × 1 (Q5T011) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.97 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 A; PDBConstruct 1–380; UniProt 1–380

GATOR1 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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain B; UniProt 1–569 Not recorded GATOR1 complex protein NPRL2 × 1 (Q8WTW4) GATOR1 complex protein DEPDC5 × 1 (O75140) KICSTOR complex protein SZT2 × 1 (Q5T011) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.97 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 B; PDBConstruct 1–569; UniProt 1–569

GATOR1 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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain C; UniProt 1–1603 Not recorded GATOR1 complex protein NPRL2 × 1 (Q8WTW4) GATOR1 complex protein NPRL3 × 1 (Q12980) KICSTOR complex protein SZT2 × 1 (Q5T011) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.97 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 C; PDBConstruct 1–1603; UniProt 1–1603

KICSTOR complex protein SZT2

Homo sapiens

UniProt Q5T011

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain D; UniProt 1–3432 Not recorded GATOR1 complex protein NPRL2 × 1 (Q8WTW4) GATOR1 complex protein NPRL3 × 1 (Q12980) GATOR1 complex protein DEPDC5 × 1 (O75140) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.97 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 SZT2_HUMAN
Isoform
PDB entities 4
Chains and sequence ranges Author chain D; PDBConstruct 1–3432; UniProt 1–3432

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 9v0j

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9v0j
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9v0j
Deposition date deposition_date2025-05-18
Structure title titleCryo-EM structure of GATOR1-KICSTOR complex
Keywords keywordsGAP, SIGNALING PROTEIN; SIGNALING PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier52.02
Radius of gyration Rg (electron density) rg_electron51.93
Forward intensity I(0) i0589299000.00
Molecular weight molecular_weight208250.0 kDa
Excluded volume excluded_volume263010 ų
Envelope volume envelope_volume414020 ų
Hydration-shell volume shell_volume68923 ų
Envelope diameter envelope_diameter191.4
Shell Rg shell_rg52.16
Envelope Rg envelope_rg51.57
Shape Rg shape_rg52.00
Total Rg total_rg51.65
Total atoms total_atoms14747
Residues n_residues2023
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 dmax183.5
Rg (real space) rg_real52.31
Rg uncertainty (real space) rg_real_error2.32
I(0) (real space) i0_real5.8930e+08
I(0) uncertainty (real space) i0_real_error1.2890e+07
Rg (reciprocal space) rg_reciprocal51.78
I(0) (reciprocal space) i0_reciprocal588900000.0000
Solution quality estimate total_estimate0.8536
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary55.1
Skewness Skewness skewness0.501
Kurtosis Kurtosis kurtosis-0.234
Angular range angular_range— – 0.1500 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha34910000.0000
Real-space data points n_real_points31
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.789; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.975; Smooth: 0.753

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)