9mip

CryoEM structure of the Protein Phasphatase 2A (Aalpha-B56gamma-Calpha) holoenzyme complex

Method: ELECTRON MICROSCOPY Dmax: 114.2 Å Quality: EXCELLENT

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

Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A alpha isoform

Homo sapiens

UniProt P30153

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain A; UniProt 1–589 Not recorded Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit gamma isoform × 1 (Q13362) Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoform × 1 (P67775) MN MANGANESE (II) ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.40 Å

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.

34 other PDB entries and 44 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name 2AAA_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–589; UniProt 1–589

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain B; UniProt 1–524 Not recorded Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A alpha isoform × 1 (P30153) Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoform × 1 (P67775) MN MANGANESE (II) ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.40 Å

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 2
Chains and sequence ranges Author chain B; PDBConstruct 1–524; UniProt 1–524

Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoform

Homo sapiens

UniProt P67775

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain C; UniProt 1–309 Not recorded Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A alpha isoform × 1 (P30153) Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit gamma isoform × 1 (Q13362) MN MANGANESE (II) ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.40 Å

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.

49 other PDB entries and 61 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PP2AA_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 1–309; UniProt 1–309

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 9mip

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id9mip
Deposition date deposition_date2024-12-13
Structure title titleCryoEM structure of the Protein Phasphatase 2A (Aalpha-B56gamma-Calpha) holoenzyme complex
Keywords keywordsPP2A, Phosphatase, Complex, Holoenzyme, Heterotrimer, HYDROLASE; HYDROLASE
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier37.76
Radius of gyration Rg (electron density) rg_electron37.09
Forward intensity I(0) i0322982000.00
Molecular weight molecular_weight149950.0 kDa
Excluded volume excluded_volume189370 ų
Envelope volume envelope_volume250980 ų
Hydration-shell volume shell_volume55220 ų
Envelope diameter envelope_diameter122.0
Shell Rg shell_rg44.59
Envelope Rg envelope_rg36.08
Shape Rg shape_rg37.07
Total Rg total_rg37.66
Total atoms total_atoms10549
Residues n_residues1312
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 dmax114.2
Rg (real space) rg_real37.49
Rg uncertainty (real space) rg_real_error0.74
I(0) (real space) i0_real3.2300e+08
I(0) uncertainty (real space) i0_real_error4.9260e+06
Rg (reciprocal space) rg_reciprocal37.66
I(0) (reciprocal space) i0_reciprocal323000000.0000
Solution quality estimate total_estimate0.9069
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary51.6
Skewness Skewness skewness0.016
Kurtosis Kurtosis kurtosis-0.612
Angular range angular_range— – 0.2100 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha35100000.0000
Real-space data points n_real_points43
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.952; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.984; Smooth: 0.946

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)