2jak

Human PP2A regulatory subunit B56g

Method: X-RAY DIFFRACTION Dmax: 87.2 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 monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 11–380 Fragment:RESIDUES 11-380 No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:29% MPD 0.1M TRIS, PH 8.0 20MM L-PROLINE Resolution 2.60 Å R-free 0.260

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 23–392; UniProt 11–380

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 2jak

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id2jak
Deposition date deposition_date2006-11-29
Structure title titleHuman PP2A regulatory subunit B56g
Keywords keywordsB56G, PP2A, PPP2R5C, PHOSPHORYLATION, PP2A REGULATORY SUBUNIT, NUCLEAR PROTEIN; NUCLEAR PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier25.29
Radius of gyration Rg (electron density) rg_electron24.75
Forward intensity I(0) i020745300.00
Molecular weight molecular_weight37802.0 kDa
Excluded volume excluded_volume48527 ų
Envelope volume envelope_volume58963 ų
Hydration-shell volume shell_volume21029 ų
Envelope diameter envelope_diameter91.5
Shell Rg shell_rg30.47
Envelope Rg envelope_rg25.15
Shape Rg shape_rg24.72
Total Rg total_rg25.60
Total atoms total_atoms2676
Residues n_residues327
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 dmax87.2
Rg (real space) rg_real25.46
Rg uncertainty (real space) rg_real_error0.77
I(0) (real space) i0_real2.0750e+07
I(0) uncertainty (real space) i0_real_error3.2350e+05
Rg (reciprocal space) rg_reciprocal25.41
I(0) (reciprocal space) i0_reciprocal20740000.0000
Solution quality estimate total_estimate0.8246
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary22.1
Skewness Skewness skewness0.494
Kurtosis Kurtosis kurtosis-0.377
Angular range angular_range— – 0.3150 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha7546000.0000
Real-space data points n_real_points64
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.719; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.655; Smooth: 0.906

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd2jaka1
Class classa — All alpha proteins
Fold Fold folda.118 — alpha-alpha superhelix
Superfamily Superfamily superfamilya.118.1 — ARM repeat
Family Family familya.118.1.20 — B56-like

CATH v4.4 (1 domains)

Domain ID domain_id2jakA00
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)