9vuy

NMR Structure of LC3B in complex with HBx BH3-like motif

Method: SOLUTION NMR Dmax: 50.1 Å Quality: GOOD

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

Microtubule-associated protein 1 light chain 3 beta

Homo sapiens

UniProt Q9GZQ8

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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 1–119 Not recorded HBx BH3-like motif × 1 (Q913A9) SOLUTION NMR NMR measurement conditions:pH 7;298 K;Ionic strength (raw mmCIF value) 50;Pressure 1 NMR sample composition:0.4 mM [U-13C; U-15N] LC3B, 0.5 mM [U-13C; U-15N] HBx BH3-like motif, 95% H2O/5% D2O | 95% H2O/5% D2O NMR sample composition:0.8 mM 1H LC3B, 0.4 mM [U-13, U-15N] HBx BH3-like motif, 95% H2O/5% D2O | 95% H2O/5% D2O NMR sample composition:0.4 mM [U-15N] LC3B, 0.5 mM [U-15N] HBx BH3-like motif, 95% H2O/5% D2O | 95% H2O/5% D2O NMR sample composition:0.5 mM [U-13, U-15N] LC3B, 0.625 mM 1H HBx BH3-like motif, 95% H2O/5% D2O | 95% H2O/5% D2O Resolution not provided

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.

49 other PDB entries and 64 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name MLP3B_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–119; UniProt 1–119

HBx BH3-like motif

Hepatitis B virus

UniProt Q913A9

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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 116–127 Not recorded Microtubule-associated protein 1 light chain 3 beta × 1 (Q9GZQ8) SOLUTION NMR NMR measurement conditions:pH 7;298 K;Ionic strength (raw mmCIF value) 50;Pressure 1 NMR sample composition:0.4 mM [U-13C; U-15N] LC3B, 0.5 mM [U-13C; U-15N] HBx BH3-like motif, 95% H2O/5% D2O | 95% H2O/5% D2O NMR sample composition:0.8 mM 1H LC3B, 0.4 mM [U-13, U-15N] HBx BH3-like motif, 95% H2O/5% D2O | 95% H2O/5% D2O NMR sample composition:0.4 mM [U-15N] LC3B, 0.5 mM [U-15N] HBx BH3-like motif, 95% H2O/5% D2O | 95% H2O/5% D2O NMR sample composition:0.5 mM [U-13, U-15N] LC3B, 0.625 mM 1H HBx BH3-like motif, 95% H2O/5% D2O | 95% H2O/5% D2O Resolution not provided

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.

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence
UniProt name X_HBVC7
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 3–14; UniProt 116–127

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 9vuy

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9vuy
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id9vuy
Deposition date deposition_date2025-07-14
最后修订 last_revision2026-05-27
Structure title titleNMR Structure of LC3B in complex with HBx BH3-like motif
Keywords keywordsComplex, HBx, LC3B, VIRAL PROTEIN; VIRAL PROTEIN
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier15.92
Radius of gyration Rg (electron density) rg_electron15.33
Forward intensity I(0) i01296060000.00
Molecular weight molecular_weight313460.0 kDa
Excluded volume excluded_volume395520 ų
Envelope volume envelope_volume40131 ų
Hydration-shell volume shell_volume18608 ų
Envelope diameter envelope_diameter55.5
Shell Rg shell_rg24.27
Envelope Rg envelope_rg18.35
Shape Rg shape_rg15.29
Total Rg total_rg15.62
Total atoms total_atoms44280
Residues n_residues2660
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 dmax50.1
Rg (real space) rg_real15.82
Rg uncertainty (real space) rg_real_error0.22
I(0) (real space) i0_real1.2960e+09
I(0) uncertainty (real space) i0_real_error1.2720e+07
Rg (reciprocal space) rg_reciprocal15.83
I(0) (reciprocal space) i0_reciprocal1296000000.0000
Solution quality estimate total_estimate0.8919
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary19.0
Skewness Skewness skewness0.084
Kurtosis Kurtosis kurtosis-0.414
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha464400.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.871; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.991; Smooth: 0.985

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

8. Citations (1)

9. Files and Curves (10)