8twi

Cryo-EM structure of the PP2A:B55-FAM122A complex, PP2Ac body

Method: ELECTRON MICROSCOPY Dmax: 82.5 Å Quality: REASONABLE

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 9–589 Not recorded Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoform × 1 (P67775) PPP2R1A-PPP2R2A-interacting phosphatase regulator 1 × 1 (Q96E09) FE FE (III) ION × 1 ZN ZINC ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8;CHAPSO was added only immediately prior to vitrification cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.69 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 4–584; UniProt 9–589

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 Non-standard monomer:Yes (specific site not provided by mmCIF) Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A alpha isoform × 1 (P30153) PPP2R1A-PPP2R2A-interacting phosphatase regulator 1 × 1 (Q96E09) FE FE (III) ION × 1 ZN ZINC ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8;CHAPSO was added only immediately prior to vitrification cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.69 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 2
Chains and sequence ranges Author chain C; PDBConstruct 3–311; UniProt 1–309

PPP2R1A-PPP2R2A-interacting phosphatase regulator 1

Homo sapiens

UniProt Q96E09

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 D; UniProt 29–120 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) FE FE (III) ION × 1 ZN ZINC ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8;CHAPSO was added only immediately prior to vitrification cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.69 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.

2 other PDB entries and 2 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PBIR1_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain D; PDBConstruct 4–95; UniProt 29–120

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 8twi

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id8twi
Deposition date deposition_date2023-08-21
Structure title titleCryo-EM structure of the PP2A:B55-FAM122A complex, PP2Ac body
Keywords keywordsProtein Phosphatase 2A:B55 holoenzyme FAM122A inhibitor substrate binding cell cycle regulation, SIGNALING PROTEIN; SIGNALING PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier25.45
Radius of gyration Rg (electron density) rg_electron24.61
Forward intensity I(0) i055797400.00
Molecular weight molecular_weight58039.0 kDa
Excluded volume excluded_volume72584 ų
Envelope volume envelope_volume85549 ų
Hydration-shell volume shell_volume29041 ų
Envelope diameter envelope_diameter85.3
Shell Rg shell_rg31.72
Envelope Rg envelope_rg24.89
Shape Rg shape_rg24.61
Total Rg total_rg25.41
Total atoms total_atoms8096
Residues n_residues510
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 dmax82.5
Rg (real space) rg_real25.43
Rg uncertainty (real space) rg_real_error0.40
I(0) (real space) i0_real5.5800e+07
I(0) uncertainty (real space) i0_real_error7.1420e+05
Rg (reciprocal space) rg_reciprocal25.44
I(0) (reciprocal space) i0_reciprocal55800000.0000
Solution quality estimate total_estimate0.7036
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary29.3
Skewness Skewness skewness0.336
Kurtosis Kurtosis kurtosis-0.381
Angular range angular_range— – 0.3100 −1
Current regularization parameter α current_alpha0.0001
Highest regularization parameter α highest_alpha14990000.0000
Real-space data points n_real_points63
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.890; Stabil: 1.000; Sysdev: 0.164; Positv: 1.000; Valcen: 0.998; Smooth: 0.981

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

8. Citations (2)

9. Files and Curves (10)