9i0o

Cryo-EM structure of human sortilin ectodomain in complex with a thyroglobulin C-terminal peptide

Method: ELECTRON MICROSCOPY Dmax: 84.8 Å Quality: REASONABLE

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

Sortilin

Homo sapiens

UniProt Q99523

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Other combination Heteromer Protein × 2 其他Polymer 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 34–756 Not recorded Thyroglobulin × 1 (P01266) 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 2 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.36 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.

16 other PDB entries and 19 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SORT_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–723; UniProt 34–756

Thyroglobulin

OrganismNot specified

UniProt P01266

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Other combination Heteromer Protein × 2 其他Polymer 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 2749–2768 Not recorded Sortilin × 1 (Q99523) 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 2 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.36 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.

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

View Construct and Data Evidence
UniProt name THYG_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–20; UniProt 2749–2768

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 9i0o

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9i0o
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9i0o
Deposition date deposition_date2025-01-15
Structure title titleCryo-EM structure of human sortilin ectodomain in complex with a thyroglobulin C-terminal peptide
Keywords keywordsTrafficking, Vacuolar Protein Sorting, VPS10, Beta propeller, Neurotensin binding receptor 3, thyroglobulin, MEMBRANE PROTEIN; MEMBRANE PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier28.37
Radius of gyration Rg (electron density) rg_electron27.02
Forward intensity I(0) i087664100.00
Molecular weight molecular_weight71773.0 kDa
Excluded volume excluded_volume89113 ų
Envelope volume envelope_volume118380 ų
Hydration-shell volume shell_volume35461 ų
Envelope diameter envelope_diameter86.3
Shell Rg shell_rg35.49
Envelope Rg envelope_rg26.64
Shape Rg shape_rg27.00
Total Rg total_rg27.96
Total atoms total_atoms9876
Residues n_residues636
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 dmax84.8
Rg (real space) rg_real28.33
Rg uncertainty (real space) rg_real_error0.14
I(0) (real space) i0_real8.5310e+07
I(0) uncertainty (real space) i0_real_error8.9170e+05
Rg (reciprocal space) rg_reciprocal28.21
I(0) (reciprocal space) i0_reciprocal87670000.0000
Solution quality estimate total_estimate0.7289
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary39.4
Skewness Skewness skewness0.092
Kurtosis Kurtosis kurtosis-0.513
Angular range angular_range— – 0.2800 −1
Current regularization parameter α current_alpha5.6640
Highest regularization parameter α highest_alpha18500000.0000
Real-space data points n_real_points57
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.965; Stabil: 0.924; Sysdev: 0.000; Positv: 1.000; Valcen: 0.989; Smooth: 0.839

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)