5vau

Bcl-2 complex with Beclin 1 BH3 domain

Method: X-RAY DIFFRACTION Dmax: 117.9 Å Quality: REASONABLE

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

Apoptosis regulator Bcl-2 -- Bcl-2-like protein 1 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 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 1–34 Chain A; UniProt 92–207 Not recorded Beclin-1 × 1 (Q14457) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 5.5;293 K;0.1M Bis-tris chloride, pH 5.5, ).2M ammonium acetate, 25% PEG 3350 Resolution 1.75 Å R-free 0.215
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 1–34 Chain B; UniProt 92–207 Not recorded Beclin-1 × 1 (Q14457) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 5.5;293 K;0.1M Bis-tris chloride, pH 5.5, ).2M ammonium acetate, 25% PEG 3350 Resolution 1.75 Å R-free 0.215
3 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain C; UniProt 1–34 Chain C; UniProt 92–207 Not recorded Beclin-1 × 1 (Q14457) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 5.5;293 K;0.1M Bis-tris chloride, pH 5.5, ).2M ammonium acetate, 25% PEG 3350 Resolution 1.75 Å R-free 0.215
4 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain D; UniProt 1–34 Chain D; UniProt 92–207 Not recorded Beclin-1 × 1 (Q14457) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 5.5;293 K;0.1M Bis-tris chloride, pH 5.5, ).2M ammonium acetate, 25% PEG 3350 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.

47 other PDB entries and 76 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 3–36; UniProt 1–34 Author chain A; PDBConstruct 53–168; UniProt 92–207 Author chain B; PDBConstruct 3–36; UniProt 1–34 Author chain B; PDBConstruct 53–168; UniProt 92–207 Author chain C; PDBConstruct 3–36; UniProt 1–34 Author chain C; PDBConstruct 53–168; UniProt 92–207 Author chain D; PDBConstruct 3–36; UniProt 1–34 Author chain D; PDBConstruct 53–168; UniProt 92–207

Beclin-1

OrganismNot specified

UniProt Q14457

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 E; UniProt 105–130 Not recorded Apoptosis regulator Bcl-2 -- Bcl-2-like protein 1 Chimera × 1 (P10415) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 5.5;293 K;0.1M Bis-tris chloride, pH 5.5, ).2M ammonium acetate, 25% PEG 3350 Resolution 1.75 Å R-free 0.215
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain F; UniProt 105–130 Not recorded Apoptosis regulator Bcl-2 -- Bcl-2-like protein 1 Chimera × 1 (P10415) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 5.5;293 K;0.1M Bis-tris chloride, pH 5.5, ).2M ammonium acetate, 25% PEG 3350 Resolution 1.75 Å R-free 0.215
3 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain G; UniProt 105–130 Not recorded Apoptosis regulator Bcl-2 -- Bcl-2-like protein 1 Chimera × 1 (P10415) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 5.5;293 K;0.1M Bis-tris chloride, pH 5.5, ).2M ammonium acetate, 25% PEG 3350 Resolution 1.75 Å R-free 0.215
4 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain H; UniProt 105–130 Not recorded Apoptosis regulator Bcl-2 -- Bcl-2-like protein 1 Chimera × 1 (P10415) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 5.5;293 K;0.1M Bis-tris chloride, pH 5.5, ).2M ammonium acetate, 25% PEG 3350 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.

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

View Construct and Data Evidence
UniProt name BECN1_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain E; PDBConstruct 1–26; UniProt 105–130 Author chain F; PDBConstruct 1–26; UniProt 105–130 Author chain G; PDBConstruct 1–26; UniProt 105–130 Author chain H; PDBConstruct 1–26; UniProt 105–130

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 5vau

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 5vau
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2. Structure Basics 2. Structure Basics

Entry ID entry_id5vau
Deposition date deposition_date2017-03-28
Structure title titleBcl-2 complex with Beclin 1 BH3 domain
Keywords keywordsapoptosis, Bcl-2, autophagy, Beclin 1; APOPTOSIS
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier34.93
Radius of gyration Rg (electron density) rg_electron34.64
Forward intensity I(0) i087662400.00
Molecular weight molecular_weight73932.0 kDa
Excluded volume excluded_volume91890 ų
Envelope volume envelope_volume121270 ų
Hydration-shell volume shell_volume30504 ų
Envelope diameter envelope_diameter116.7
Shell Rg shell_rg39.32
Envelope Rg envelope_rg34.03
Shape Rg shape_rg34.65
Total Rg total_rg34.95
Total atoms total_atoms5219
Residues n_residues644
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 dmax117.9
Rg (real space) rg_real35.10
Rg uncertainty (real space) rg_real_error1.05
I(0) (real space) i0_real8.7660e+07
I(0) uncertainty (real space) i0_real_error1.4860e+06
Rg (reciprocal space) rg_reciprocal35.00
I(0) (reciprocal space) i0_reciprocal87650000.0000
Solution quality estimate total_estimate0.5867
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary26.2
Skewness Skewness skewness0.352
Kurtosis Kurtosis kurtosis-0.619
Angular range angular_range— – 0.2250 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha61220000.0000
Real-space data points n_real_points46
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.775; Stabil: 1.000; Sysdev: 0.186; Positv: 1.000; Valcen: 0.739; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)