8ce0

N-terminal domain of human apolipoprotein E

Method: X-RAY DIFFRACTION Dmax: 70.9 Å Quality: REASONABLE

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

Maltodextrin-binding protein,Apolipoprotein E

Homo sapiens

UniProt A0A376KDN7

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 24–396 Not recorded GOL GLYCEROL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7;293.15 K;NaCl, Hepes, PEG 8000 Resolution 1.75 Å R-free 0.215

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.

19 other PDB entries and 32 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name A0A376KDN7_ECOLX
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–373; UniProt 24–396

Maltodextrin-binding 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 GOL GLYCEROL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7;293.15 K;NaCl, Hepes, PEG 8000 Resolution 1.75 Å R-free 0.215

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

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 8ce0

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8ce0
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8ce0
Deposition date deposition_date2023-02-01
Structure title titleN-terminal domain of human apolipoprotein E
Keywords keywordsApolipoprotein E, N-terminal domain, LIPID TRANSPORT; LIPID TRANSPORT
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier18.78
Radius of gyration Rg (electron density) rg_electron18.15
Forward intensity I(0) i05670110.00
Molecular weight molecular_weight16776.0 kDa
Excluded volume excluded_volume20862 ų
Envelope volume envelope_volume24712 ų
Hydration-shell volume shell_volume12725 ų
Envelope diameter envelope_diameter71.0
Shell Rg shell_rg22.58
Envelope Rg envelope_rg18.72
Shape Rg shape_rg18.15
Total Rg total_rg18.93
Total atoms total_atoms1178
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 dmax70.9
Rg (real space) rg_real18.99
Rg uncertainty (real space) rg_real_error0.63
I(0) (real space) i0_real5.6700e+06
I(0) uncertainty (real space) i0_real_error8.0760e+04
Rg (reciprocal space) rg_reciprocal18.96
I(0) (reciprocal space) i0_reciprocal5670000.0000
Solution quality estimate total_estimate0.7491
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary18.4
Skewness Skewness skewness0.658
Kurtosis Kurtosis kurtosis0.051
Angular range angular_range— – 0.4250 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha1591000.0000
Real-space data points n_real_points74
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.418; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.537; Smooth: 0.944

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)