9j5r

Pathogen effector forms a phosphatase holoenzyme complex with host core enzyme to promote disease

Method: ELECTRON MICROSCOPY Dmax: 133.1 Å Quality: GOOD

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

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

Arabidopsis thaliana

UniProt Q38950

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 1–587 Not recorded RxLR effector protein PSR2 × 1 (E0W4V5) Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoform × 1 (P67775) MN MANGANESE (II) ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.30 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.

4 other PDB entries and 4 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name 2AAB_ARATH
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–587; UniProt 1–587

RxLR effector protein PSR2

Phytophthora sojae

UniProt E0W4V5

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 1–670 Not recorded Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A beta isoform × 1 (Q38950) Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoform × 1 (P67775) MN MANGANESE (II) ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.30 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.

5 other PDB entries and 5 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PSR2_PHYSO
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–670; UniProt 1–670

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 beta isoform × 1 (Q38950) RxLR effector protein PSR2 × 1 (E0W4V5) MN MANGANESE (II) ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.30 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 9j5r

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9j5r
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9j5r
Deposition date deposition_date2024-08-13
Structure title titlePathogen effector forms a phosphatase holoenzyme complex with host core enzyme to promote disease
Keywords keywordspathogen; PP2A core enzyme; virulent function; susceptibility, PLANT PROTEIN; PLANT PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier38.28
Radius of gyration Rg (electron density) rg_electron38.18
Forward intensity I(0) i0233972000.00
Molecular weight molecular_weight121130.0 kDa
Excluded volume excluded_volume150620 ų
Envelope volume envelope_volume222490 ų
Hydration-shell volume shell_volume50128 ų
Envelope diameter envelope_diameter141.4
Shell Rg shell_rg42.58
Envelope Rg envelope_rg38.02
Shape Rg shape_rg38.20
Total Rg total_rg38.43
Total atoms total_atoms8531
Residues n_residues1192
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 dmax133.1
Rg (real space) rg_real38.37
Rg uncertainty (real space) rg_real_error1.33
I(0) (real space) i0_real2.3400e+08
I(0) uncertainty (real space) i0_real_error3.6690e+06
Rg (reciprocal space) rg_reciprocal38.32
I(0) (reciprocal space) i0_reciprocal234000000.0000
Solution quality estimate total_estimate0.8524
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary48.7
Skewness Skewness skewness0.431
Kurtosis Kurtosis kurtosis0.038
Angular range angular_range— – 0.2050 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha24630000.0000
Real-space data points n_real_points42
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.756; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.990; Smooth: 0.820

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)