8t8r

Sortilin-PGRN peptide complex

Method: X-RAY DIFFRACTION Dmax: 96.0 Å Quality: GOOD

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 79–756 Not recorded Paragranulin peptide × 1 (P28799) beta-D-mannopyranose-(1-4)-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 × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;293 K;20.00 %w/ PEG 3350, 0.20 M Sodium citrate Resolution 2.87 Å R-free 0.287

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 1–678; UniProt 79–756

Paragranulin peptide

OrganismNot specified

UniProt P28799

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 578–593 Not recorded Sortilin × 1 (Q99523) beta-D-mannopyranose-(1-4)-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 × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;293 K;20.00 %w/ PEG 3350, 0.20 M Sodium citrate Resolution 2.87 Å R-free 0.287

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.

7 other PDB entries and 8 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name GRN_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–16; UniProt 578–593

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 8t8r

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8t8r
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id8t8r
Deposition date deposition_date2023-06-23
Structure title titleSortilin-PGRN peptide complex
Keywords keywordsSortilin, Progranulin, TRANSPORT PROTEIN; TRANSPORT PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier28.64
Radius of gyration Rg (electron density) rg_electron27.47
Forward intensity I(0) i096238000.00
Molecular weight molecular_weight75546.0 kDa
Excluded volume excluded_volume93886 ų
Envelope volume envelope_volume124250 ų
Hydration-shell volume shell_volume36705 ų
Envelope diameter envelope_diameter104.0
Shell Rg shell_rg35.69
Envelope Rg envelope_rg27.47
Shape Rg shape_rg27.44
Total Rg total_rg28.40
Total atoms total_atoms5316
Residues n_residues662
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 dmax96.0
Rg (real space) rg_real28.51
Rg uncertainty (real space) rg_real_error0.64
I(0) (real space) i0_real9.6240e+07
I(0) uncertainty (real space) i0_real_error1.3490e+06
Rg (reciprocal space) rg_reciprocal28.57
I(0) (reciprocal space) i0_reciprocal96240000.0000
Solution quality estimate total_estimate0.8818
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary38.4
Skewness Skewness skewness0.152
Kurtosis Kurtosis kurtosis-0.427
Angular range angular_range— – 0.2750 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha21200000.0000
Real-space data points n_real_points56
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.828; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.998; Smooth: 0.978

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)