7adt

Orf virus Apoptosis inhibitor ORFV125

Method: X-RAY DIFFRACTION Dmax: 69.0 Å Quality: GOOD

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

Apoptosis inhibitor

Orf virus

UniProt A0A0R8HV90

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 1–143 Chain B; UniProt 1–143 Not recorded Apoptosis regulator BAX × 2 (Q07812) EDO 1,2-ETHANEDIOL × 7 GOL GLYCEROL × 2 MG MAGNESIUM ION × 41 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 5.5;293 K;0.2 M Magnesium chloride hexahydrate, 0.1 M Bis-Tris pH 5.5, 25% PEG 3350 Resolution 2.21 Å R-free 0.259

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.

3 other PDB entries and 4 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name A0A0R8HV90_ORFV
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 6–148; UniProt 1–143 Author chain B; PDBConstruct 6–148; UniProt 1–143

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 C; UniProt 50–77 Chain U; UniProt 50–77 Not recorded Apoptosis inhibitor × 2 (A0A0R8HV90) EDO 1,2-ETHANEDIOL × 7 GOL GLYCEROL × 2 MG MAGNESIUM ION × 41 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 5.5;293 K;0.2 M Magnesium chloride hexahydrate, 0.1 M Bis-Tris pH 5.5, 25% PEG 3350 Resolution 2.21 Å R-free 0.259

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 2
Chains and sequence ranges Author chain C; PDBConstruct 1–28; UniProt 50–77 Author chain U; 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 7adt

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7adt
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7adt
Deposition date deposition_date2020-09-16
Structure title titleOrf virus Apoptosis inhibitor ORFV125
Keywords keywordsOrf virus, Apoptosis, Bcl-2, ITC; APOPTOSIS
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier22.13
Radius of gyration Rg (electron density) rg_electron20.89
Forward intensity I(0) i024353900.00
Molecular weight molecular_weight35716.0 kDa
Excluded volume excluded_volume43925 ų
Envelope volume envelope_volume53894 ų
Hydration-shell volume shell_volume21736 ų
Envelope diameter envelope_diameter70.8
Shell Rg shell_rg27.23
Envelope Rg envelope_rg21.22
Shape Rg shape_rg20.86
Total Rg total_rg21.80
Total atoms total_atoms4878
Residues n_residues310
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 dmax69.0
Rg (real space) rg_real22.10
Rg uncertainty (real space) rg_real_error0.47
I(0) (real space) i0_real2.4350e+07
I(0) uncertainty (real space) i0_real_error3.2220e+05
Rg (reciprocal space) rg_reciprocal22.11
I(0) (reciprocal space) i0_reciprocal24350000.0000
Solution quality estimate total_estimate0.8237
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary24.7
Skewness Skewness skewness0.318
Kurtosis Kurtosis kurtosis-0.449
Angular range angular_range— – 0.3600 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha7046000.0000
Real-space data points n_real_points68
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.904; Stabil: 0.998; Sysdev: 1.000; Positv: 1.000; Valcen: 0.996; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

8. Citations (1)

9. Files and Curves (10)