13fr

Cholesterol complex of the START domain of Caenorhabditis elegans StAR-related lipid transfer protein 3 (STARD3)

Method: X-RAY DIFFRACTION Dmax: 104.3 Å Quality: EXCELLENT

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

START domain-containing protein

Caenorhabditis elegans

UniProt Q19819

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 monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 221–447 Not recorded GOL GLYCEROL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;293 K;50 mM sodium cacodylate pH 6.5, 100 mM magnesium acetate, 200 mM potassium chloride, 14% w/v PEG 8000 Resolution 2.09 Å R-free 0.243
2 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain B; UniProt 221–447 Not recorded GOL GLYCEROL × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;293 K;50 mM sodium cacodylate pH 6.5, 100 mM magnesium acetate, 200 mM potassium chloride, 14% w/v PEG 8000 Resolution 2.09 Å R-free 0.243
3 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain C; UniProt 221–447 Not recorded CLR CHOLESTEROL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;293 K;50 mM sodium cacodylate pH 6.5, 100 mM magnesium acetate, 200 mM potassium chloride, 14% w/v PEG 8000 Resolution 2.09 Å R-free 0.243
4 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain D; UniProt 221–447 Not recorded CLR CHOLESTEROL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;293 K;50 mM sodium cacodylate pH 6.5, 100 mM magnesium acetate, 200 mM potassium chloride, 14% w/v PEG 8000 Resolution 2.09 Å R-free 0.243

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.

1 other PDB entries and 2 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name Q19819_CAEEL
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 2–228; UniProt 221–447 Author chain B; PDBConstruct 2–228; UniProt 221–447 Author chain C; PDBConstruct 2–228; UniProt 221–447 Author chain D; PDBConstruct 2–228; UniProt 221–447

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 13fr

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 13fr
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2. Structure Basics 2. Structure Basics

Entry ID entry_id13fr
Deposition date deposition_date2026-05-04
最后修订 last_revision2026-05-13
Structure title titleCholesterol complex of the START domain of Caenorhabditis elegans StAR-related lipid transfer protein 3 (STARD3)
Keywords keywordscholesterol, cholesterol traffic, cholesterol metabolism, physical biochemistry, STARD3, START domain, NPC1/NPC2, LIPID TRANSPORT; LIPID TRANSPORT
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier32.82
Radius of gyration Rg (electron density) rg_electron32.06
Forward intensity I(0) i0149970000.00
Molecular weight molecular_weight99428.0 kDa
Excluded volume excluded_volume125200 ų
Envelope volume envelope_volume160200 ų
Hydration-shell volume shell_volume41092 ų
Envelope diameter envelope_diameter110.1
Shell Rg shell_rg39.46
Envelope Rg envelope_rg31.77
Shape Rg shape_rg32.03
Total Rg total_rg32.77
Total atoms total_atoms7001
Residues n_residues851
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 dmax104.3
Rg (real space) rg_real32.70
Rg uncertainty (real space) rg_real_error0.64
I(0) (real space) i0_real1.5000e+08
I(0) uncertainty (real space) i0_real_error2.2580e+06
Rg (reciprocal space) rg_reciprocal32.76
I(0) (reciprocal space) i0_reciprocal150000000.0000
Solution quality estimate total_estimate0.9054
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary41.3
Skewness Skewness skewness0.179
Kurtosis Kurtosis kurtosis-0.593
Angular range angular_range— – 0.2400 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha51400000.0000
Real-space data points n_real_points49
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.941; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.998; Smooth: 0.945

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)