8ax9

Human Apolipoprotein E4 (ApoE4) N-terminal domain (space group P212121)

Method: X-RAY DIFFRACTION Dmax: 67.9 Å Quality: GOOD

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

Maltose/maltodextrin-binding periplasmic protein,Apolipoprotein E

Homo sapiens

UniProt P02649

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 19–317 Not recorded No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.5;293.15 K;HEPES, PEG3350 Resolution 1.55 Å R-free 0.195

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.

28 other PDB entries and 30 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name APOE_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 377–675; UniProt 19–317

Maltose/maltodextrin-binding periplasmic protein,Apolipoprotein E

Homo sapiens

UniProt P0AEX9

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 24–392 Not recorded No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.5;293.15 K;HEPES, PEG3350 Resolution 1.55 Å R-free 0.195

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.

366 other PDB entries and 491 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name MALE_ECOLI
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–369; UniProt 24–392

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 8ax9

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8ax9
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8ax9
Deposition date deposition_date2022-08-31
Structure title titleHuman Apolipoprotein E4 (ApoE4) N-terminal domain (space group P212121)
Keywords keywordsApolipoprotein E, 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_guinier18.69
Radius of gyration Rg (electron density) rg_electron18.09
Forward intensity I(0) i05556150.00
Molecular weight molecular_weight16684.0 kDa
Excluded volume excluded_volume20745 ų
Envelope volume envelope_volume24290 ų
Hydration-shell volume shell_volume12592 ų
Envelope diameter envelope_diameter68.2
Shell Rg shell_rg22.40
Envelope Rg envelope_rg18.56
Shape Rg shape_rg18.08
Total Rg total_rg18.82
Total atoms total_atoms1172
Residues n_residues143
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 dmax67.9
Rg (real space) rg_real18.89
Rg uncertainty (real space) rg_real_error0.59
I(0) (real space) i0_real5.5560e+06
I(0) uncertainty (real space) i0_real_error7.1240e+04
Rg (reciprocal space) rg_reciprocal18.86
I(0) (reciprocal space) i0_reciprocal5556000.0000
Solution quality estimate total_estimate0.7797
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary17.7
Skewness Skewness skewness0.637
Kurtosis Kurtosis kurtosis-0.011
Angular range angular_range— – 0.4250 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha1410000.0000
Real-space data points n_real_points74
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.505; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.668; Smooth: 0.948

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

8. Citations (1)

9. Files and Curves (10)