8a50

Crystal structure of HSF2BP-ALPHA1 tetramer

Method: X-RAY DIFFRACTION Dmax: 51.8 Å Quality: REASONABLE

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

Heat shock factor 2-binding protein

OrganismNot specified

UniProt O75031

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 homooligomer Homooligomer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 19–50 Chain B; UniProt 19–50 Not recorded PO4 PHOSPHATE ION × 4 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;277 K;0.2 M LiCl 0.1 M sodium acetate trihydrate pH 5 20% PEG6000 Resolution 1.48 Å R-free 0.217

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 3 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name HSF2B_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–32; UniProt 19–50 Author chain B; PDBConstruct 1–32; UniProt 19–50

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 8a50

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8a50
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8a50
Deposition date deposition_date2022-06-13
Structure title titleCrystal structure of HSF2BP-ALPHA1 tetramer
Keywords keywordsComplex, RECOMBINATION; RECOMBINATION
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier15.67
Radius of gyration Rg (electron density) rg_electron14.72
Forward intensity I(0) i01246540.00
Molecular weight molecular_weight7394.0 kDa
Excluded volume excluded_volume9308 ų
Envelope volume envelope_volume12433 ų
Hydration-shell volume shell_volume7893 ų
Envelope diameter envelope_diameter51.8
Shell Rg shell_rg18.77
Envelope Rg envelope_rg14.69
Shape Rg shape_rg14.74
Total Rg total_rg15.71
Total atoms total_atoms1065
Residues n_residues59
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 dmax51.8
Rg (real space) rg_real15.65
Rg uncertainty (real space) rg_real_error0.37
I(0) (real space) i0_real1.2470e+06
I(0) uncertainty (real space) i0_real_error1.3560e+04
Rg (reciprocal space) rg_reciprocal15.66
I(0) (reciprocal space) i0_reciprocal1247000.0000
Solution quality estimate total_estimate0.6153
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary20.3
Skewness Skewness skewness0.178
Kurtosis Kurtosis kurtosis-0.231
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha63340.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.634; Stabil: 0.999; Sysdev: 0.368; Positv: 1.000; Valcen: 0.993; 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)