6iyy

Crystal structure of human WIPI3,loop deletion mutant

Method: X-RAY DIFFRACTION Dmax: 61.1 Å Quality: EXCELLENT

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 monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 8–344 Mutation:DELETION OF RESIDUES 75-80 and 264-281 SO4 SULFATE ION × 7 X-RAY DIFFRACTION X-ray crystallization conditions:EVAPORATION;pH 7;289 K;1.6M Ammonium Sulfate, 0.1M Tris-HCl Resolution 1.80 Å R-free 0.204

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 5–317; UniProt 8–344

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 6iyy

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6iyy
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id6iyy
Deposition date deposition_date2018-12-17
Structure title titleCrystal structure of human WIPI3,loop deletion mutant
Keywords keywordsMEMBRANE BOUND PROTEIN, LIPID BINDING PROTEIN; LIPID BINDING PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier20.00
Radius of gyration Rg (electron density) rg_electron18.83
Forward intensity I(0) i021836700.00
Molecular weight molecular_weight34753.0 kDa
Excluded volume excluded_volume43063 ų
Envelope volume envelope_volume50064 ų
Hydration-shell volume shell_volume21608 ų
Envelope diameter envelope_diameter62.1
Shell Rg shell_rg25.85
Envelope Rg envelope_rg18.97
Shape Rg shape_rg18.84
Total Rg total_rg19.72
Total atoms total_atoms2431
Residues n_residues312
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 dmax61.1
Rg (real space) rg_real19.82
Rg uncertainty (real space) rg_real_error0.25
I(0) (real space) i0_real2.1840e+07
I(0) uncertainty (real space) i0_real_error2.3050e+05
Rg (reciprocal space) rg_reciprocal19.85
I(0) (reciprocal space) i0_reciprocal21840000.0000
Solution quality estimate total_estimate0.9003
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary26.2
Skewness Skewness skewness0.091
Kurtosis Kurtosis kurtosis-0.472
Angular range angular_range— – 0.3950 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha4937000.0000
Real-space data points n_real_points71
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.914; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.977; Smooth: 0.979

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)