6trr

Structural insight into tanapoxvirus mediated inhibition of apoptosis

Method: X-RAY DIFFRACTION Dmax: 69.7 Å Quality: GOOD

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

16L protein

Yaba-like disease virus

UniProt Q9DHU6

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 1–147 Not recorded Apoptosis regulator BAX × 2 (Q07812) NA SODIUM ION × 4 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 4;293 K;1.0 M Lithium Chloride, 0.1 M Citrate pH 4.0 20% PEG 6000 Resolution 2.12 Å R-free 0.254

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.

2 other PDB entries and 2 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name Q9DHU6_YLDV
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 6–152; UniProt 1–147

Apoptosis regulator BAX

OrganismNot specified

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 B; UniProt 50–77 Not recorded 16L protein × 2 (Q9DHU6) NA SODIUM ION × 4 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 4;293 K;1.0 M Lithium Chloride, 0.1 M Citrate pH 4.0 20% PEG 6000 Resolution 2.12 Å R-free 0.254

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 Q07812-8
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–28; UniProt 50–77

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 6trr

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6trr
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6trr
Deposition date deposition_date2019-12-19
Structure title titleStructural insight into tanapoxvirus mediated inhibition of apoptosis
Keywords keywordsPox virus, Apoptosis, Bcl-2; APOPTOSIS
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier18.53
Radius of gyration Rg (electron density) rg_electron17.45
Forward intensity I(0) i06234240.00
Molecular weight molecular_weight18611.0 kDa
Excluded volume excluded_volume23580 ų
Envelope volume envelope_volume29071 ų
Hydration-shell volume shell_volume14765 ų
Envelope diameter envelope_diameter69.2
Shell Rg shell_rg22.68
Envelope Rg envelope_rg17.74
Shape Rg shape_rg17.43
Total Rg total_rg18.45
Total atoms total_atoms2601
Residues n_residues161
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 dmax69.7
Rg (real space) rg_real18.55
Rg uncertainty (real space) rg_real_error0.75
I(0) (real space) i0_real6.2340e+06
I(0) uncertainty (real space) i0_real_error8.9970e+04
Rg (reciprocal space) rg_reciprocal18.55
I(0) (reciprocal space) i0_reciprocal6234000.0000
Solution quality estimate total_estimate0.8148
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary22.0
Skewness Skewness skewness0.453
Kurtosis Kurtosis kurtosis0.217
Angular range angular_range— – 0.4300 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha674800.0000
Real-space data points n_real_points74
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.559; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.911; Smooth: 0.999

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_id6trrA01
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)