8ese

Crystal structure of human Vps29 bound to a peptide from Vps35L

Method: X-RAY DIFFRACTION Dmax: 51.2 Å Quality: EXCELLENT

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

VPS35 endosomal protein-sorting factor-like

Homo sapiens

UniProt B3KT69

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 X; UniProt 16–38 Not recorded Vacuolar protein sorting-associated protein 29 × 1 (Q9UBQ0) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5.5;293 K;0.1 M Bis-tris pH 5.5 and 25% (w/v) PEG3350 Resolution 1.35 Å R-free 0.241

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.

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence
UniProt name B3KT69_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain X; PDBConstruct 1–23; UniProt 16–38

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 Z; UniProt 1–182 Not recorded VPS35 endosomal protein-sorting factor-like × 1 (B3KT69) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5.5;293 K;0.1 M Bis-tris pH 5.5 and 25% (w/v) PEG3350 Resolution 1.35 Å R-free 0.241

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 34 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name VPS29_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain Z; PDBConstruct 3–184; UniProt 1–182

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 8ese

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8ese
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8ese
Deposition date deposition_date2022-10-13
Structure title titleCrystal structure of human Vps29 bound to a peptide from Vps35L
Keywords keywordsCommander, Retriever, Vps29, Vps35L, ENDOCYTOSIS; ENDOCYTOSIS
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier17.11
Radius of gyration Rg (electron density) rg_electron15.80
Forward intensity I(0) i08320370.00
Molecular weight molecular_weight22301.0 kDa
Excluded volume excluded_volume28381 ų
Envelope volume envelope_volume31544 ų
Hydration-shell volume shell_volume16383 ų
Envelope diameter envelope_diameter50.9
Shell Rg shell_rg22.28
Envelope Rg envelope_rg16.10
Shape Rg shape_rg15.79
Total Rg total_rg16.94
Total atoms total_atoms3160
Residues n_residues198
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 dmax51.2
Rg (real space) rg_real16.97
Rg uncertainty (real space) rg_real_error0.24
I(0) (real space) i0_real8.3200e+06
I(0) uncertainty (real space) i0_real_error9.1990e+04
Rg (reciprocal space) rg_reciprocal16.99
I(0) (reciprocal space) i0_reciprocal8320000.0000
Solution quality estimate total_estimate0.9053
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary22.2
Skewness Skewness skewness0.042
Kurtosis Kurtosis kurtosis-0.509
Angular range angular_range— – 0.4650 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha1849000.0000
Real-space data points n_real_points77
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.931; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.978; Smooth: 0.995

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 1 domains

CATH v4.4 (1 domains)

Domain ID domain_id8eseZ01
Class class3 — Alpha Beta
Architecture architecture60 — 4-Layer Sandwich
Topology topology21 — Purple Acid Phosphatase; chain A, domain 2
Homologous superfamily homologous superfamily10 — Metallo-dependent phosphatases

8. Citations (1)

9. Files and Curves (10)