8uwb

Crystal structure of PP2A PPP2R1A-PPP2CA-PPP2R5E phosphatase.

Method: X-RAY DIFFRACTION Dmax: 173.8 Å Quality: GOOD

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

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 Chain F; UniProt 1–309 Not recorded Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit epsilon isoform × 1 (Q16537) Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A alpha isoform × 1 (P30153) MN MANGANESE (II) ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 5.77;297 K;23% (w/v) PEG 20k, 0.1 M BIS-TRIS pH 5.77 Resolution 3.15 Å R-free 0.263
2 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain C; UniProt 1–309 Chain F; UniProt 1–309 Not recorded Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit epsilon isoform × 1 (Q16537) Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A alpha isoform × 1 (P30153) MN MANGANESE (II) ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 5.77;297 K;23% (w/v) PEG 20k, 0.1 M BIS-TRIS pH 5.77 Resolution 3.15 Å R-free 0.263

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 60 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PP2AA_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain C; PDBConstruct 25–333; UniProt 1–309 Author chain F; PDBConstruct 25–333; UniProt 1–309

Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit epsilon isoform

Homo sapiens

UniProt Q16537

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 1–467 Not recorded Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoform × 1 (P67775) Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A alpha isoform × 1 (P30153) MN MANGANESE (II) ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 5.77;297 K;23% (w/v) PEG 20k, 0.1 M BIS-TRIS pH 5.77 Resolution 3.15 Å R-free 0.263
2 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain E; UniProt 1–467 Not recorded Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoform × 1 (P67775) Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A alpha isoform × 1 (P30153) MN MANGANESE (II) ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 5.77;297 K;23% (w/v) PEG 20k, 0.1 M BIS-TRIS pH 5.77 Resolution 3.15 Å R-free 0.263

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 2A5E_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–467; UniProt 1–467 Author chain E; PDBConstruct 1–467; UniProt 1–467

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 Chain D; UniProt 1–589 Not recorded Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoform × 1 (P67775) Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit epsilon isoform × 1 (Q16537) MN MANGANESE (II) ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 5.77;297 K;23% (w/v) PEG 20k, 0.1 M BIS-TRIS pH 5.77 Resolution 3.15 Å R-free 0.263
2 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain A; UniProt 1–589 Chain D; UniProt 1–589 Not recorded Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoform × 1 (P67775) Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit epsilon isoform × 1 (Q16537) MN MANGANESE (II) ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 5.77;297 K;23% (w/v) PEG 20k, 0.1 M BIS-TRIS pH 5.77 Resolution 3.15 Å R-free 0.263

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 43 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name 2AAA_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain A; PDBConstruct 24–612; UniProt 1–589 Author chain D; PDBConstruct 24–612; UniProt 1–589

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 8uwb

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8uwb
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id8uwb
Deposition date deposition_date2023-11-06
Structure title titleCrystal structure of PP2A PPP2R1A-PPP2CA-PPP2R5E phosphatase.
Keywords keywordsPP2A, protein phosphatase, Serine/threonine-protein phosphatase 2A, B56epsilon, CELL CYCLE; CELL CYCLE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier53.47
Radius of gyration Rg (electron density) rg_electron53.67
Forward intensity I(0) i01202330000.00
Molecular weight molecular_weight296660.0 kDa
Excluded volume excluded_volume374060 ų
Envelope volume envelope_volume543200 ų
Hydration-shell volume shell_volume85029 ų
Envelope diameter envelope_diameter176.4
Shell Rg shell_rg56.11
Envelope Rg envelope_rg51.90
Shape Rg shape_rg53.62
Total Rg total_rg53.93
Total atoms total_atoms20851
Residues n_residues2597
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 dmax173.8
Rg (real space) rg_real53.49
Rg uncertainty (real space) rg_real_error1.60
I(0) (real space) i0_real1.2020e+09
I(0) uncertainty (real space) i0_real_error2.2350e+07
Rg (reciprocal space) rg_reciprocal53.43
I(0) (reciprocal space) i0_reciprocal1202000000.0000
Solution quality estimate total_estimate0.8695
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary59.9
Skewness Skewness skewness0.290
Kurtosis Kurtosis kurtosis-0.561
Angular range angular_range— – 0.1450 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha57960000.0000
Real-space data points n_real_points30
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.911; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.999; Smooth: 0.568

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)