5swf

The structure of the PP2A B56 subunit double phosphorylated BubR1 complex

Method: X-RAY DIFFRACTION Dmax: 90.9 Å Quality: REASONABLE

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 62–411 Fragment:UNP residues 62-411 Double phosphorylated BubR1 × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.75;298 K;8% PEG 8k, 0.8 M HEPES, 0.8 M LiCl Resolution 2.82 Å R-free 0.231

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 Q13362-5
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 6–355; UniProt 62–411

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 5swf

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 5swf
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2. Structure Basics 2. Structure Basics

Entry ID entry_id5swf
Deposition date deposition_date2016-08-08
Structure title titleThe structure of the PP2A B56 subunit double phosphorylated BubR1 complex
Keywords keywordsPhosphatase, Regulator, SLiM, cell cycle, Hydrolase; Hydrolase, cell cycle
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier25.46
Radius of gyration Rg (electron density) rg_electron24.88
Forward intensity I(0) i022082800.00
Molecular weight molecular_weight38618.0 kDa
Excluded volume excluded_volume49424 ų
Envelope volume envelope_volume59210 ų
Hydration-shell volume shell_volume21340 ų
Envelope diameter envelope_diameter95.4
Shell Rg shell_rg30.09
Envelope Rg envelope_rg25.18
Shape Rg shape_rg24.86
Total Rg total_rg25.60
Total atoms total_atoms2731
Residues n_residues330
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 dmax90.9
Rg (real space) rg_real25.67
Rg uncertainty (real space) rg_real_error0.82
I(0) (real space) i0_real2.2080e+07
I(0) uncertainty (real space) i0_real_error3.2130e+05
Rg (reciprocal space) rg_reciprocal25.61
I(0) (reciprocal space) i0_reciprocal22080000.0000
Solution quality estimate total_estimate0.6107
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary23.5
Skewness Skewness skewness0.556
Kurtosis Kurtosis kurtosis-0.220
Angular range angular_range— – 0.3100 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha5528000.0000
Real-space data points n_real_points63
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.638; Stabil: 1.000; Sysdev: 0.164; Positv: 1.000; Valcen: 0.721; Smooth: 0.806

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 1 domains

CATH v4.4 (1 domains)

Domain ID domain_id5swfA00
Class class1 — Mainly Alpha
Architecture architecture25 — Alpha Horseshoe
Topology topology10 — Leucine-rich Repeat Variant
Homologous superfamily homologous superfamily10 — Leucine-rich Repeat Variant

8. Citations (1)

9. Files and Curves (10)