9v86

Cryo-EM structure of KICSTOR CCC complex (state 3)

Method: ELECTRON MICROSCOPY Dmax: 216.8 Å Quality: REASONABLE

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

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 A; UniProt 1–3432 Not recorded KICSTOR complex protein ITFG2 × 1 (Q969R8) KICSTOR complex protein kaptin × 1 (Q9Y664) KICSTOR subunit 2 × 1 (Q96MD2) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.04 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 1
Chains and sequence ranges Author chain A; PDBConstruct 1–3432; UniProt 1–3432

KICSTOR complex protein ITFG2

Homo sapiens

UniProt Q969R8

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 1–447 Not recorded KICSTOR complex protein SZT2 × 1 (Q5T011) KICSTOR complex protein kaptin × 1 (Q9Y664) KICSTOR subunit 2 × 1 (Q96MD2) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.04 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.

5 other PDB entries and 5 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ITFG2_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–447; UniProt 1–447

KICSTOR complex protein kaptin

Homo sapiens

UniProt Q9Y664

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 1–436 Not recorded KICSTOR complex protein SZT2 × 1 (Q5T011) KICSTOR complex protein ITFG2 × 1 (Q969R8) KICSTOR subunit 2 × 1 (Q96MD2) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.04 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.

5 other PDB entries and 5 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name KPTN_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 1–436; UniProt 1–436

KICSTOR subunit 2

Homo sapiens

UniProt Q96MD2

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 1–445 Not recorded KICSTOR complex protein SZT2 × 1 (Q5T011) KICSTOR complex protein ITFG2 × 1 (Q969R8) KICSTOR complex protein kaptin × 1 (Q9Y664) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.04 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.

4 other PDB entries and 4 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name KICS2_HUMAN
Isoform
PDB entities 4
Chains and sequence ranges Author chain D; PDBConstruct 1–445; UniProt 1–445

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 9v86

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9v86
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id9v86
Deposition date deposition_date2025-05-29
Structure title titleCryo-EM structure of KICSTOR CCC complex (state 3)
Keywords keywordslipid binding protein, SIGNALING PROTEIN; SIGNALING PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier70.99
Radius of gyration Rg (electron density) rg_electron71.65
Forward intensity I(0) i0560733000.00
Molecular weight molecular_weight198750.0 kDa
Excluded volume excluded_volume248810 ų
Envelope volume envelope_volume459850 ų
Hydration-shell volume shell_volume61850 ų
Envelope diameter envelope_diameter250.2
Shell Rg shell_rg53.20
Envelope Rg envelope_rg72.79
Shape Rg shape_rg71.82
Total Rg total_rg70.52
Total atoms total_atoms14073
Residues n_residues1992
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 dmax216.8
Rg (real space) rg_real71.34
Rg uncertainty (real space) rg_real_error1.83
I(0) (real space) i0_real5.5910e+08
I(0) uncertainty (real space) i0_real_error1.2330e+07
Rg (reciprocal space) rg_reciprocal67.56
I(0) (reciprocal space) i0_reciprocal556100000.0000
Solution quality estimate total_estimate0.7131
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary39.4
Skewness Skewness skewness0.545
Kurtosis Kurtosis kurtosis-0.772
Angular range angular_range— – 0.1100 −1
Current regularization parameter α current_alpha0.0371
Highest regularization parameter α highest_alpha17290000.0000
Real-space data points n_real_points23
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.571; Stabil: 0.998; Sysdev: 1.000; Positv: 1.000; Valcen: 0.554; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)