7k36

Cryo-EM structure of STRIPAK complex

Method: ELECTRON MICROSCOPY Dmax: 196.8 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 × 9 PDB declaration: nonameric(9) Consistent with protein copy count Chain A; UniProt 1–589 Not recorded Striatin-3 × 5 (Q13033) Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoform × 1 (P67775) MOB-like protein phocein × 1 (Q9Y3A3) Striatin-interacting protein 1 × 1 (Q5VSL9) MN MANGANESE (II) ION × 2 ZN ZINC ION × 2 IHP INOSITOL HEXAKISPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.30 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.

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 1–589; UniProt 1–589

Striatin-3

Homo sapiens

UniProt Q13033

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 × 9 PDB declaration: nonameric(9) Consistent with protein copy count Chain B; UniProt 1–713 Chain D; UniProt 1–713 Chain E; UniProt 1–713 Chain F; UniProt 1–713 Chain G; UniProt 1–713 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) MOB-like protein phocein × 1 (Q9Y3A3) Striatin-interacting protein 1 × 1 (Q5VSL9) MN MANGANESE (II) ION × 2 ZN ZINC ION × 2 IHP INOSITOL HEXAKISPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.30 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.

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

View Construct and Data Evidence
UniProt name STRN3_HUMAN
Isoform Q13033-2
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–713; UniProt 1–713 Author chain D; PDBConstruct 1–713; UniProt 1–713 Author chain E; PDBConstruct 1–713; UniProt 1–713 Author chain F; PDBConstruct 1–713; UniProt 1–713 Author chain G; PDBConstruct 1–713; UniProt 1–713

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 × 9 PDB declaration: nonameric(9) Consistent with protein copy count Chain C; UniProt 1–309 Not recorded Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A alpha isoform × 1 (P30153) Striatin-3 × 5 (Q13033) MOB-like protein phocein × 1 (Q9Y3A3) Striatin-interacting protein 1 × 1 (Q5VSL9) MN MANGANESE (II) ION × 2 ZN ZINC ION × 2 IHP INOSITOL HEXAKISPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.30 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

MOB-like protein phocein

Homo sapiens

UniProt Q9Y3A3

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 × 9 PDB declaration: nonameric(9) Consistent with protein copy count Chain H; UniProt 1–225 Not recorded Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A alpha isoform × 1 (P30153) Striatin-3 × 5 (Q13033) Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoform × 1 (P67775) Striatin-interacting protein 1 × 1 (Q5VSL9) MN MANGANESE (II) ION × 2 ZN ZINC ION × 2 IHP INOSITOL HEXAKISPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.30 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.

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

View Construct and Data Evidence
UniProt name PHOCN_HUMAN
Isoform
PDB entities 4
Chains and sequence ranges Author chain H; PDBConstruct 1–225; UniProt 1–225

Striatin-interacting protein 1

Homo sapiens

UniProt Q5VSL9

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 × 9 PDB declaration: nonameric(9) Consistent with protein copy count Chain I; UniProt 1–837 Not recorded Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A alpha isoform × 1 (P30153) Striatin-3 × 5 (Q13033) Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoform × 1 (P67775) MOB-like protein phocein × 1 (Q9Y3A3) MN MANGANESE (II) ION × 2 ZN ZINC ION × 2 IHP INOSITOL HEXAKISPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.30 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.

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

View Construct and Data Evidence
UniProt name STRP1_HUMAN
Isoform
PDB entities 5
Chains and sequence ranges Author chain I; PDBConstruct 1–837; UniProt 1–837

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 7k36

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7k36
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7k36
Deposition date deposition_date2020-09-10
Structure title titleCryo-EM structure of STRIPAK complex
Keywords keywordsphosphorylation, complex, PP2A, SIGNALING PROTEIN; SIGNALING PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier59.34
Radius of gyration Rg (electron density) rg_electron59.81
Forward intensity I(0) i0808352000.00
Molecular weight molecular_weight235930.0 kDa
Excluded volume excluded_volume294520 ų
Envelope volume envelope_volume448450 ų
Hydration-shell volume shell_volume67335 ų
Envelope diameter envelope_diameter209.5
Shell Rg shell_rg53.08
Envelope Rg envelope_rg60.33
Shape Rg shape_rg59.92
Total Rg total_rg59.25
Total atoms total_atoms16613
Residues n_residues2183
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 dmax196.8
Rg (real space) rg_real60.22
Rg uncertainty (real space) rg_real_error2.45
I(0) (real space) i0_real8.0830e+08
I(0) uncertainty (real space) i0_real_error1.8400e+07
Rg (reciprocal space) rg_reciprocal58.57
I(0) (reciprocal space) i0_reciprocal806200000.0000
Solution quality estimate total_estimate0.7974
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks0
Primary peak position r_peak_primary
Skewness Skewness skewness0.609
Kurtosis Kurtosis kurtosis-0.267
Angular range angular_range— – 0.1300 −1
Current regularization parameter α current_alpha0.0001
Highest regularization parameter α highest_alpha25340000.0000
Real-space data points n_real_points27
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.807; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.922; Smooth: 0.019

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (8)

7. Fold Classification (SCOP + CATH) 3 domains

CATH v4.4 (3 domains)

Domain ID domain_id7k36A01
Class class1 — Mainly Alpha
Architecture architecture25 — Alpha Horseshoe
Topology topology10 — Leucine-rich Repeat Variant
Homologous superfamily homologous superfamily10 — Leucine-rich Repeat Variant
Domain ID domain_id7k36C01
Class class3 — Alpha Beta
Architecture architecture60 — 4-Layer Sandwich
Topology topology21 — Purple Acid Phosphatase; chain A, domain 2
Homologous superfamily homologous superfamily10 — Metallo-dependent phosphatases
Domain ID domain_id7k36H01
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology140 — Butyryl-CoA Dehydrogenase, subunit A; domain 3
Homologous superfamily homologous superfamily30 — MOB kinase activator

8. Citations (1)

9. Files and Curves (10)