2wh6

Crystal structure of anti-apoptotic BHRF1 in complex with the Bim BH3 domain

Method: X-RAY DIFFRACTION Dmax: 51.1 Å Quality: EXCELLENT

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

EARLY ANTIGEN PROTEIN R

Epstein-barr virus strain ag876

UniProt P03182

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 1–160 Fragment:BCL-2, RESIDUES 1-160 BCL-2-LIKE PROTEIN 11 × 1 (O43521) BR BROMIDE ION × 9 GOL GLYCEROL × 2 X-RAY DIFFRACTION X-ray crystallization conditions:pH 4;0.1 M MALIC ACID PH 4 1.25 M NABR Resolution 1.50 Å R-free 0.205

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.

6 other PDB entries and 14 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name EAR_EBV
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 14–173; UniProt 1–160

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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 51–76 Fragment:BH3, RESIDUES 51-72 EARLY ANTIGEN PROTEIN R × 1 (P03182) BR BROMIDE ION × 9 GOL GLYCEROL × 2 X-RAY DIFFRACTION X-ray crystallization conditions:pH 4;0.1 M MALIC ACID PH 4 1.25 M NABR Resolution 1.50 Å R-free 0.205

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
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–26; UniProt 51–76

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 2wh6

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2wh6
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2wh6
Deposition date deposition_date2009-05-01
Structure title titleCrystal structure of anti-apoptotic BHRF1 in complex with the Bim BH3 domain
Keywords keywordsMITOCHONDRION, EARLY PROTEIN, TRANSMEMBRANE, VIRAL PROTEIN, APOPTOSIS; APOPTOSIS
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier16.90
Radius of gyration Rg (electron density) rg_electron15.34
Forward intensity I(0) i09836060.00
Molecular weight molecular_weight21592.0 kDa
Excluded volume excluded_volume26144 ų
Envelope volume envelope_volume29121 ų
Hydration-shell volume shell_volume15637 ų
Envelope diameter envelope_diameter50.3
Shell Rg shell_rg21.75
Envelope Rg envelope_rg15.59
Shape Rg shape_rg15.27
Total Rg total_rg16.54
Total atoms total_atoms1478
Residues n_residues179
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 dmax51.1
Rg (real space) rg_real16.76
Rg uncertainty (real space) rg_real_error0.18
I(0) (real space) i0_real9.8360e+06
I(0) uncertainty (real space) i0_real_error1.0260e+05
Rg (reciprocal space) rg_reciprocal16.78
I(0) (reciprocal space) i0_reciprocal9836000.0000
Solution quality estimate total_estimate0.9012
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary22.2
Skewness Skewness skewness0.057
Kurtosis Kurtosis kurtosis-0.457
Angular range angular_range— – 0.4700 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha2029000.0000
Real-space data points n_real_points77
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.914; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.975; Smooth: 0.996

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

7. Fold Classification (SCOP + CATH) 1 domains

CATH v4.4 (1 domains)

Domain ID domain_id2wh6A00
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)