8vwx

Human Bcl-2 (G101V Mutant)/Bcl-xL Chimera Fused to Maltose-Binding Protein

Method: X-RAY DIFFRACTION Dmax: 80.3 Å Quality: EXCELLENT

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

Maltose/maltodextrin-binding periplasmic protein fused to apoptosis regulator Bcl-2/Bcl-xL chimera

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 27–392 Mutation:G101V No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8.5;277 K;100 mM Tris (pH 8.5), 25% PEG 3350, and 200 mM sodium chloride Resolution 1.77 Å R-free 0.225

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 19–384; UniProt 27–392

Maltose/maltodextrin-binding periplasmic protein fused to apoptosis regulator Bcl-2/Bcl-xL chimera

Homo sapiens

UniProt P10415

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 10–34 Chain A; UniProt 92–207 Mutation:G101V No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8.5;277 K;100 mM Tris (pH 8.5), 25% PEG 3350, and 200 mM sodium chloride Resolution 1.77 Å R-free 0.225

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.

47 other PDB entries and 79 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name BCL2_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 391–415; UniProt 10–34 Author chain A; PDBConstruct 432–547; UniProt 92–207

Maltose/maltodextrin-binding periplasmic protein fused to apoptosis regulator Bcl-2/Bcl-xL chimera

Homo sapiens

UniProt Q07817

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 29–44 Mutation:G101V No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8.5;277 K;100 mM Tris (pH 8.5), 25% PEG 3350, and 200 mM sodium chloride Resolution 1.77 Å R-free 0.225

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.

123 other PDB entries and 195 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name B2CL1_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 416–431; UniProt 29–44

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 8vwx

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id8vwx
Deposition date deposition_date2024-02-02
Structure title titleHuman Bcl-2 (G101V Mutant)/Bcl-xL Chimera Fused to Maltose-Binding Protein
Keywords keywordsApoptosis, Bcl-2, G101V Mutant, MBP Fusion, Bcl-xL Chimera; APOPTOSIS
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier25.71
Radius of gyration Rg (electron density) rg_electron24.62
Forward intensity I(0) i048727100.00
Molecular weight molecular_weight55817.0 kDa
Excluded volume excluded_volume70421 ų
Envelope volume envelope_volume84927 ų
Hydration-shell volume shell_volume28572 ų
Envelope diameter envelope_diameter81.3
Shell Rg shell_rg32.10
Envelope Rg envelope_rg24.59
Shape Rg shape_rg24.59
Total Rg total_rg25.56
Total atoms total_atoms3950
Residues n_residues502
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 dmax80.3
Rg (real space) rg_real25.63
Rg uncertainty (real space) rg_real_error0.46
I(0) (real space) i0_real4.8730e+07
I(0) uncertainty (real space) i0_real_error6.3620e+05
Rg (reciprocal space) rg_reciprocal25.66
I(0) (reciprocal space) i0_reciprocal48730000.0000
Solution quality estimate total_estimate0.9075
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary28.5
Skewness Skewness skewness0.207
Kurtosis Kurtosis kurtosis-0.534
Angular range angular_range— – 0.3100 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha12740000.0000
Real-space data points n_real_points63
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.943; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.999; Smooth: 0.964

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

8. Citations (1)

9. Files and Curves (10)