9gnj

Crystal structure of a PP2A B56gamma double phosphorylated BRCA2 complex

Method: X-RAY DIFFRACTION Dmax: 95.5 Å Quality: GOOD

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

Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit gamma isoform

Homo sapiens

UniProt Q13362

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 30–380 Not recorded BRCA2 × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293 K;18% de PEG3350, 100mM Bis-Tris propane, 200 mM de Sodium Citrate Resolution 2.85 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.

20 other PDB entries and 25 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name 2A5G_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 2–352; UniProt 30–380

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 9gnj

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9gnj
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9gnj
Deposition date deposition_date2024-09-03
最后修订 last_revision2025-09-24
Structure title titleCrystal structure of a PP2A B56gamma double phosphorylated BRCA2 complex
Keywords keywordsComplex, SIGNALING PROTEIN; SIGNALING PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier25.82
Radius of gyration Rg (electron density) rg_electron25.35
Forward intensity I(0) i023650400.00
Molecular weight molecular_weight40002.0 kDa
Excluded volume excluded_volume51208 ų
Envelope volume envelope_volume62677 ų
Hydration-shell volume shell_volume22115 ų
Envelope diameter envelope_diameter97.7
Shell Rg shell_rg30.58
Envelope Rg envelope_rg26.00
Shape Rg shape_rg25.33
Total Rg total_rg26.09
Total atoms total_atoms2825
Residues n_residues336
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 dmax95.5
Rg (real space) rg_real26.06
Rg uncertainty (real space) rg_real_error0.94
I(0) (real space) i0_real2.3650e+07
I(0) uncertainty (real space) i0_real_error3.4920e+05
Rg (reciprocal space) rg_reciprocal25.99
I(0) (reciprocal space) i0_reciprocal23650000.0000
Solution quality estimate total_estimate0.7909
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary23.5
Skewness Skewness skewness0.595
Kurtosis Kurtosis kurtosis-0.106
Angular range angular_range— – 0.3050 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha6086000.0000
Real-space data points n_real_points62
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.567; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.596; Smooth: 0.982

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

8. Citations (1)

9. Files and Curves (10)