5f0k

Structure of VPS35 N terminal region

Method: X-RAY DIFFRACTION Dmax: 128.0 Å Quality: GOOD

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

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 monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 14–470 Fragment:Residues 14-470 EDO 1,2-ETHANEDIOL × 5 GOL GLYCEROL × 1 SO4 SULFATE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.6;291 K;1.7 M AmSO4, 2% PEG 1000, 0.1 M Hepes pH 7.6 Resolution 3.07 Å R-free 0.255
2 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain B; UniProt 14–470 Fragment:Residues 14-470 EDO 1,2-ETHANEDIOL × 2 GOL GLYCEROL × 3 SO4 SULFATE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.6;291 K;1.7 M AmSO4, 2% PEG 1000, 0.1 M Hepes pH 7.6 Resolution 3.07 Å R-free 0.255
3 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain C; UniProt 14–470 Fragment:Residues 14-470 EDO 1,2-ETHANEDIOL × 2 GOL GLYCEROL × 1 PG4 TETRAETHYLENE GLYCOL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.6;291 K;1.7 M AmSO4, 2% PEG 1000, 0.1 M Hepes pH 7.6 Resolution 3.07 Å R-free 0.255
4 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain D; UniProt 14–470 Fragment:Residues 14-470 EDO 1,2-ETHANEDIOL × 3 GOL GLYCEROL × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.6;291 K;1.7 M AmSO4, 2% PEG 1000, 0.1 M Hepes pH 7.6 Resolution 3.07 Å R-free 0.255
5 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain E; UniProt 14–470 Fragment:Residues 14-470 EDO 1,2-ETHANEDIOL × 2 GOL GLYCEROL × 2 SO4 SULFATE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.6;291 K;1.7 M AmSO4, 2% PEG 1000, 0.1 M Hepes pH 7.6 Resolution 3.07 Å R-free 0.255

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 24 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name VPS35_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 6–462; UniProt 14–470 Author chain B; PDBConstruct 6–462; UniProt 14–470 Author chain C; PDBConstruct 6–462; UniProt 14–470 Author chain D; PDBConstruct 6–462; UniProt 14–470 Author chain E; PDBConstruct 6–462; UniProt 14–470

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 5f0k

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 5f0k
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id5f0k
Deposition date deposition_date2015-11-27
Structure title titleStructure of VPS35 N terminal region
Keywords keywordsprotein transport, retromer, sorting nexin; PROTEIN TRANSPORT
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier43.71
Radius of gyration Rg (electron density) rg_electron42.88
Forward intensity I(0) i0881620000.00
Molecular weight molecular_weight250960.0 kDa
Excluded volume excluded_volume317120 ų
Envelope volume envelope_volume471410 ų
Hydration-shell volume shell_volume87426 ų
Envelope diameter envelope_diameter134.8
Shell Rg shell_rg52.43
Envelope Rg envelope_rg41.04
Shape Rg shape_rg42.90
Total Rg total_rg43.29
Total atoms total_atoms35584
Residues n_residues2158
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 dmax128.0
Rg (real space) rg_real43.33
Rg uncertainty (real space) rg_real_error0.56
I(0) (real space) i0_real8.8160e+08
I(0) uncertainty (real space) i0_real_error1.5040e+07
Rg (reciprocal space) rg_reciprocal43.70
I(0) (reciprocal space) i0_reciprocal882000000.0000
Solution quality estimate total_estimate0.8975
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary64.0
Skewness Skewness skewness-0.110
Kurtosis Kurtosis kurtosis-0.652
Angular range angular_range— – 0.1800 −1
Current regularization parameter α current_alpha0.0001
Highest regularization parameter α highest_alpha113100000.0000
Real-space data points n_real_points37
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.926; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.957; Smooth: 0.927

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

8. Citations (1)

9. Files and Curves (10)