9c7t

PP2A:B55-Eya3 substrate complex

Method: ELECTRON MICROSCOPY Dmax: 117.6 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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 9–589 Fragment:residues 9-589 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) Eyes absent homolog 3 × 1 (Q99504) FE2 FE (II) ION × 1 ZN ZINC ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.70 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) Eyes absent homolog 3 × 1 (Q99504) FE2 FE (II) ION × 1 ZN ZINC ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.70 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 6–451; 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) Eyes absent homolog 3 × 1 (Q99504) FE2 FE (II) ION × 1 ZN ZINC ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.70 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

Eyes absent homolog 3

Homo sapiens

UniProt Q99504

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 62–108 Fragment:residues 62-108 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) FE2 FE (II) ION × 1 ZN ZINC ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.70 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.

1 other PDB entries and 1 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name EYA3_HUMAN
Isoform
PDB entities 4
Chains and sequence ranges Author chain D; PDBConstruct 4–50; UniProt 62–108

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 9c7t

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9c7t
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9c7t
Deposition date deposition_date2024-06-11
Structure title titlePP2A:B55-Eya3 substrate complex
Keywords keywordsPP2A:B55, Eya3, substrate complex, HYDROLASE, HYDROLASE-SUBSTRATE complex; HYDROLASE/SUBSTRATE
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier37.93
Radius of gyration Rg (electron density) rg_electron37.23
Forward intensity I(0) i0348585000.00
Molecular weight molecular_weight151710.0 kDa
Excluded volume excluded_volume189740 ų
Envelope volume envelope_volume249160 ų
Hydration-shell volume shell_volume54400 ų
Envelope diameter envelope_diameter129.4
Shell Rg shell_rg44.82
Envelope Rg envelope_rg36.55
Shape Rg shape_rg37.20
Total Rg total_rg37.76
Total atoms total_atoms10659
Residues n_residues1332
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 dmax117.6
Rg (real space) rg_real37.69
Rg uncertainty (real space) rg_real_error0.79
I(0) (real space) i0_real3.4860e+08
I(0) uncertainty (real space) i0_real_error5.7190e+06
Rg (reciprocal space) rg_reciprocal37.84
I(0) (reciprocal space) i0_reciprocal348600000.0000
Solution quality estimate total_estimate0.6876
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary53.2
Skewness Skewness skewness0.047
Kurtosis Kurtosis kurtosis-0.610
Angular range angular_range— – 0.2100 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha58590000.0000
Real-space data points n_real_points43
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.928; Stabil: 1.000; Sysdev: 0.080; Positv: 1.000; Valcen: 0.990; Smooth: 0.918

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

8. Citations (2)

9. Files and Curves (10)