8ttb

Cryo-EM structure of the PP2A:B55-ARPP19 complex

Method: ELECTRON MICROSCOPY Dmax: 116.4 Å Quality: GOOD

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 9–589 Not recorded Serine/threonine-protein phosphatase 2A 55 kDa regulatory subunit B alpha isoform × 1 (P63151) Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoform × 1 (P67775) cAMP-regulated phosphoprotein 19 × 1 (P56211) 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 2.77 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 55 kDa regulatory subunit B alpha isoform

Homo sapiens

UniProt P63151

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain B; UniProt 2–447 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) cAMP-regulated phosphoprotein 19 × 1 (P56211) 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 2.77 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.

9 other PDB entries and 10 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name 2ABA_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 5–450; UniProt 2–447

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 × 4 PDB declaration: tetrameric(4) 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) Serine/threonine-protein phosphatase 2A 55 kDa regulatory subunit B alpha isoform × 1 (P63151) cAMP-regulated phosphoprotein 19 × 1 (P56211) 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 2.77 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 3–311; UniProt 1–309

cAMP-regulated phosphoprotein 19

Homo sapiens

UniProt P56211

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain D; UniProt 1–112 Non-standard monomer:Yes (specific site not provided by mmCIF) Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A alpha isoform × 1 (P30153) Serine/threonine-protein phosphatase 2A 55 kDa regulatory subunit B alpha isoform × 1 (P63151) 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 2.77 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.

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence
UniProt name ARP19_HUMAN
Isoform
PDB entities 4
Chains and sequence ranges Author chain D; PDBConstruct 3–114; UniProt 1–112

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 8ttb

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id8ttb
Deposition date deposition_date2023-08-13
Structure title titleCryo-EM structure of the PP2A:B55-ARPP19 complex
Keywords keywordsProtein Phosphatase 2A:B55 holoenzyme, ARPP19 inhibitor, cell cycle regulation, SIGNALING PROTEIN, HYDROLASE; SIGNALING PROTEIN,HYDROLASE
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier37.26
Radius of gyration Rg (electron density) rg_electron36.60
Forward intensity I(0) i0373650000.00
Molecular weight molecular_weight156660.0 kDa
Excluded volume excluded_volume195880 ų
Envelope volume envelope_volume251320 ų
Hydration-shell volume shell_volume55656 ų
Envelope diameter envelope_diameter128.8
Shell Rg shell_rg44.27
Envelope Rg envelope_rg35.93
Shape Rg shape_rg36.58
Total Rg total_rg37.14
Total atoms total_atoms21924
Residues n_residues1374
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 dmax116.4
Rg (real space) rg_real37.04
Rg uncertainty (real space) rg_real_error0.72
I(0) (real space) i0_real3.7360e+08
I(0) uncertainty (real space) i0_real_error5.9860e+06
Rg (reciprocal space) rg_reciprocal37.18
I(0) (reciprocal space) i0_reciprocal373700000.0000
Solution quality estimate total_estimate0.8980
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary52.6
Skewness Skewness skewness0.065
Kurtosis Kurtosis kurtosis-0.572
Angular range angular_range— – 0.2100 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha67970000.0000
Real-space data points n_real_points43
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.919; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.986; Smooth: 0.927

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

8. Citations (1)

9. Files and Curves (10)