8r02

Crystal structure of the retromer complex VPS29/VPS35 with the ligand bis-1,3-phenyl guanylhydrazone, 2a

Method: X-RAY DIFFRACTION Dmax: 126.9 Å Quality: GOOD

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

Vacuolar protein sorting-associated protein 29

Homo sapiens

UniProt Q9UBQ0

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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 1–182 Not recorded Vacuolar protein sorting-associated protein 35 × 1 (Q96QK1) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7.4;293 K;20% PEG 3350, 150 mM NaK tartrate, 100 mM NaCl, pH 7.4 Resolution 2.50 Å R-free 0.264
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 1–182 Not recorded Vacuolar protein sorting-associated protein 35 × 1 (Q96QK1) XFZ Bis-1,3-phenyl guanylhydrazon × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7.4;293 K;20% PEG 3350, 150 mM NaK tartrate, 100 mM NaCl, pH 7.4 Resolution 2.50 Å R-free 0.264

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.

20 other PDB entries and 33 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name VPS29_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 4–185; UniProt 1–182 Author chain B; PDBConstruct 4–185; UniProt 1–182

Vacuolar protein sorting-associated protein 35

Homo sapiens

UniProt Q96QK1

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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain C; UniProt 476–780 Not recorded Vacuolar protein sorting-associated protein 29 × 1 (Q9UBQ0) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7.4;293 K;20% PEG 3350, 150 mM NaK tartrate, 100 mM NaCl, pH 7.4 Resolution 2.50 Å R-free 0.264
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain D; UniProt 476–780 Not recorded Vacuolar protein sorting-associated protein 29 × 1 (Q9UBQ0) XFZ Bis-1,3-phenyl guanylhydrazon × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7.4;293 K;20% PEG 3350, 150 mM NaK tartrate, 100 mM NaCl, pH 7.4 Resolution 2.50 Å R-free 0.264

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.

12 other PDB entries and 27 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name VPS35_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain C; PDBConstruct 2–306; UniProt 476–780 Author chain D; PDBConstruct 2–306; UniProt 476–780

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 8r02

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8r02
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id8r02
Deposition date deposition_date2023-10-30
最后修订 last_revision2024-03-27
Structure title titleCrystal structure of the retromer complex VPS29/VPS35 with the ligand bis-1,3-phenyl guanylhydrazone, 2a
Keywords keywordsComplex, transport, recycling, ligand, PROTEIN TRANSPORT; PROTEIN TRANSPORT
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier37.01
Radius of gyration Rg (electron density) rg_electron36.90
Forward intensity I(0) i0178498000.00
Molecular weight molecular_weight109870.0 kDa
Excluded volume excluded_volume138380 ų
Envelope volume envelope_volume178860 ų
Hydration-shell volume shell_volume42500 ų
Envelope diameter envelope_diameter132.8
Shell Rg shell_rg40.56
Envelope Rg envelope_rg36.91
Shape Rg shape_rg36.85
Total Rg total_rg37.30
Total atoms total_atoms7747
Residues n_residues962
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 dmax126.9
Rg (real space) rg_real37.40
Rg uncertainty (real space) rg_real_error1.28
I(0) (real space) i0_real1.7850e+08
I(0) uncertainty (real space) i0_real_error3.6180e+06
Rg (reciprocal space) rg_reciprocal37.16
I(0) (reciprocal space) i0_reciprocal178500000.0000
Solution quality estimate total_estimate0.8041
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary32.5
Skewness Skewness skewness0.559
Kurtosis Kurtosis kurtosis-0.337
Angular range angular_range— – 0.2150 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha46090000.0000
Real-space data points n_real_points44
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.698; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.686; Smooth: 0.669

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)