8zqg

Crystal structure of WIPI3 in complex with ATG16L1

Method: X-RAY DIFFRACTION Dmax: 106.4 Å Quality: GOOD

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

WD repeat domain phosphoinositide-interacting protein 3

Homo sapiens

UniProt Q5MNZ6

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 8–344 Chain B; UniProt 8–344 Not recorded Autophagy-related protein 16-1 × 2 (Q676U5) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8.8;289 K;0.02 M Citric acid, 0.08 M BIS-TRIS propane (pH 8.8); 16% w/v Polyethylene glycol 3350 Resolution 2.77 Å R-free 0.233

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.

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

View Construct and Data Evidence
UniProt name WIPI3_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 5–323; UniProt 8–344 Author chain B; PDBConstruct 5–323; UniProt 8–344

Autophagy-related protein 16-1

Homo sapiens

UniProt Q676U5

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain C; UniProt 124–188 Chain D; UniProt 124–188 Not recorded WD repeat domain phosphoinositide-interacting protein 3 × 2 (Q5MNZ6) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8.8;289 K;0.02 M Citric acid, 0.08 M BIS-TRIS propane (pH 8.8); 16% w/v Polyethylene glycol 3350 Resolution 2.77 Å R-free 0.233

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.

13 other PDB entries and 24 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name A16L1_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain C; PDBConstruct 5–69; UniProt 124–188 Author chain D; PDBConstruct 5–69; UniProt 124–188

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 8zqg

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id8zqg
Deposition date deposition_date2024-06-02
Structure title titleCrystal structure of WIPI3 in complex with ATG16L1
Keywords keywordsWIPI3, ATG16L1, PROTEIN BINDING; PROTEIN BINDING
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier32.74
Radius of gyration Rg (electron density) rg_electron32.33
Forward intensity I(0) i0102184000.00
Molecular weight molecular_weight80046.0 kDa
Excluded volume excluded_volume100010 ų
Envelope volume envelope_volume127530 ų
Hydration-shell volume shell_volume34131 ų
Envelope diameter envelope_diameter110.9
Shell Rg shell_rg37.72
Envelope Rg envelope_rg31.95
Shape Rg shape_rg32.38
Total Rg total_rg32.62
Total atoms total_atoms5617
Residues n_residues725
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 dmax106.4
Rg (real space) rg_real32.86
Rg uncertainty (real space) rg_real_error0.85
I(0) (real space) i0_real1.0220e+08
I(0) uncertainty (real space) i0_real_error1.5440e+06
Rg (reciprocal space) rg_reciprocal32.81
I(0) (reciprocal space) i0_reciprocal102200000.0000
Solution quality estimate total_estimate0.8798
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary31.0
Skewness Skewness skewness0.347
Kurtosis Kurtosis kurtosis-0.633
Angular range angular_range— – 0.2400 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha17470000.0000
Real-space data points n_real_points49
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.877; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.912; Smooth: 0.891

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)