4zie

Crystal Structure of core/latch dimer of Bax in complex with BimBH3

Method: X-RAY DIFFRACTION Dmax: 78.9 Å Quality: REASONABLE

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

Apoptosis regulator BAX

Homo sapiens

UniProt Q07812

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 1–166 Mutation:C62S C126S Bcl-2-like protein 11 × 2 (O43521) EDO 1,2-ETHANEDIOL × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 9;277 K;PEG6000, bicine Resolution 1.80 Å R-free 0.229

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.

35 other PDB entries and 61 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name BAX_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–166; UniProt 1–166

Bcl-2-like protein 11

OrganismNot specified

UniProt O43521

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain C; UniProt 141–166 Fragment:BH3 motif, UNP RESIDUES 141-166 Apoptosis regulator BAX × 2 (Q07812) EDO 1,2-ETHANEDIOL × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 9;277 K;PEG6000, bicine Resolution 1.80 Å R-free 0.229

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.

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

View Construct and Data Evidence
UniProt name B2L11_HUMAN
Isoform O43521-12
PDB entities 2
Chains and sequence ranges Author chain C; PDBConstruct 1–26; UniProt 141–166

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 4zie

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4zie
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2. Structure Basics 2. Structure Basics

Entry ID entry_id4zie
Deposition date deposition_date2015-04-28
Structure title titleCrystal Structure of core/latch dimer of Bax in complex with BimBH3
Keywords keywordsBax, Apoptosis, BH3 domain, Structural Genomics; APOPTOSIS
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier23.88
Radius of gyration Rg (electron density) rg_electron23.42
Forward intensity I(0) i06350570.00
Molecular weight molecular_weight18814.0 kDa
Excluded volume excluded_volume23690 ų
Envelope volume envelope_volume33528 ų
Hydration-shell volume shell_volume13682 ų
Envelope diameter envelope_diameter80.6
Shell Rg shell_rg26.66
Envelope Rg envelope_rg24.59
Shape Rg shape_rg23.49
Total Rg total_rg23.72
Total atoms total_atoms1334
Residues n_residues169
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 dmax78.9
Rg (real space) rg_real24.38
Rg uncertainty (real space) rg_real_error0.76
I(0) (real space) i0_real6.3510e+06
I(0) uncertainty (real space) i0_real_error9.3550e+04
Rg (reciprocal space) rg_reciprocal24.27
I(0) (reciprocal space) i0_reciprocal6350000.0000
Solution quality estimate total_estimate0.7403
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary22.2
Skewness Skewness skewness0.654
Kurtosis Kurtosis kurtosis-0.422
Angular range angular_range— – 0.3350 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha377000.0000
Real-space data points n_real_points65
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.511; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.483; Smooth: 0.609

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 1 domains

CATH v4.4 (1 domains)

Domain ID domain_id4zieA00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology437 — Apoptosis Regulator Bcl-x
Homologous superfamily homologous superfamily10 — Blc2-like

8. Citations (1)

9. Files and Curves (10)