6fg9

Mouse SORCS2 ectodomain (sortilin related VPS10 domain containing receptor 2)

Method: X-RAY DIFFRACTION Dmax: 176.0 Å Quality: GOOD

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

VPS10 domain-containing receptor SorCS2

Mus musculus

UniProt Q9EPR5

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 homooligomer Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 116–1077 Chain B; UniProt 116–1077 Not recorded NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 11 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.4;291 K;0.1 M Sodium chloride, 0.02 M Tris pH 7.5, 0.1 M Magnesium chloride hexahydrate and 11 % w/v PEG 1500, final pH 6.4 Resolution 4.20 Å R-free 0.291

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 1 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SORC2_MOUSE
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 2–963; UniProt 116–1077 Author chain B; PDBConstruct 2–963; UniProt 116–1077

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 6fg9

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6fg9
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6fg9
Deposition date deposition_date2018-01-10
Structure title titleMouse SORCS2 ectodomain (sortilin related VPS10 domain containing receptor 2)
Keywords keywordsSorCS2, VPS10, transport, sorting, Sortilin, APOPTOSIS; APOPTOSIS
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier55.06
Radius of gyration Rg (electron density) rg_electron55.25
Forward intensity I(0) i0623656000.00
Molecular weight molecular_weight208680.0 kDa
Excluded volume excluded_volume261700 ų
Envelope volume envelope_volume422060 ų
Hydration-shell volume shell_volume68230 ų
Envelope diameter envelope_diameter186.7
Shell Rg shell_rg52.34
Envelope Rg envelope_rg53.47
Shape Rg shape_rg55.22
Total Rg total_rg55.25
Total atoms total_atoms14712
Residues n_residues1833
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 dmax176.0
Rg (real space) rg_real55.49
Rg uncertainty (real space) rg_real_error1.79
I(0) (real space) i0_real6.2370e+08
I(0) uncertainty (real space) i0_real_error1.2040e+07
Rg (reciprocal space) rg_reciprocal54.67
I(0) (reciprocal space) i0_reciprocal622900000.0000
Solution quality estimate total_estimate0.8052
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary42.5
Skewness Skewness skewness0.467
Kurtosis Kurtosis kurtosis-0.559
Angular range angular_range— – 0.1450 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha86590000.0000
Real-space data points n_real_points30
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.845; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.913; Smooth: 0.018

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

8. Citations (1)

9. Files and Curves (10)