← Back to search
1aep

MOLECULAR STRUCTURE OF AN APOLIPOPROTEIN DETERMINED AT 2.5-ANGSTROMS RESOLUTION

Method: X-RAY DIFFRACTION Dmax: 62.0 Å Quality: GOOD
▼

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

APOLIPOPHORIN III

Locusta migratoria

UniProt P10762

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 20–180 Not recorded No other associated polymer X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 2.70 Å

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.

Other PDB Difference from Current Entry 1AEP Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
1LS4 NMR structure of apolipophorin-III from Locusta migratoria Deposited 2002-05-16 Different construct Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 1–180（180 aa）
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 6.4；303 K；Ionic strength (raw mmCIF value) 200 mM phosphate；Pressure 1
NMR sample composition 1 mM apolipophorin-III, 15N/13C uniformly labeled, 200 mM phosphate buffer, 0.5 mM sodium Azide | 95% H2O/5% D2O
Resolution not provided

1 other PDB entries and 1 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name APL3_LOCMI
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 1–161； UniProt 20–180

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 1aep

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1aep
Download Download
▼

2. Structure Basics 2. Structure Basics

Entry ID entry_id1aep
Deposition date deposition_date1992-11-30
Structure title titleMOLECULAR STRUCTURE OF AN APOLIPOPROTEIN DETERMINED AT 2.5-ANGSTROMS RESOLUTION
Keywords keywordsLIPOPROTEIN; LIPOPROTEIN
Experimental Method methodX-RAY DIFFRACTION
▼

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

Radius of gyration Rg (Guinier) rg_guinier17.46 Å
Radius of gyration Rg (electron density) rg_electron16.61 Å
Forward intensity I(0) i05729490.00
Molecular weight molecular_weight16469.0 kDa
Excluded volume excluded_volume20263 ų
Envelope volume envelope_volume24008 ų
Hydration-shell volume shell_volume12977 ų
Envelope diameter envelope_diameter60.3 Å
Shell Rg shell_rg21.54 Å
Envelope Rg envelope_rg17.05 Å
Shape Rg shape_rg16.60 Å
Total Rg total_rg17.48 Å
Total atoms total_atoms1161
Residues n_residues153
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 Å−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 dmax62.0 Å
Rg (real space) rg_real17.53 Å
Rg uncertainty (real space) rg_real_error0.54 Å
I(0) (real space) i0_real5.7290e+06
I(0) uncertainty (real space) i0_real_error7.2720e+04
Rg (reciprocal space) rg_reciprocal17.52 Å
I(0) (reciprocal space) i0_reciprocal5729000.0000
Solution quality estimate total_estimate0.8261
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary19.0 Å
Skewness Skewness skewness0.501
Kurtosis Kurtosis kurtosis-0.052
Angular range angular_range— – 0.4550 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha1590000.0000
Real-space data points n_real_points76
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.624; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.875; Smooth: 0.990
▶

5. Crystallography and Experiment 5. Crystallography & Experiment

▶

6. Entities and Polymers Entities & Polymers (1)

▼

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd1aepa_
Class classa — All alpha proteins
Fold Fold folda.63 — Apolipophorin-III
Superfamily Superfamily superfamilya.63.1 — Apolipophorin-III
Family Family familya.63.1.1 — Apolipophorin-III

CATH v4.4 (1 domains)

Domain ID domain_id1aepA00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology120 — Four Helix Bundle (Hemerythrin (Met), subunit A)
Homologous superfamily homologous superfamily20 — Apolipoprotein
▶

8. Citations (1)

▶

9. Files and Curves (10)