6iur

A phosphatase complex STRN3-PP2Aa

Method: X-RAY DIFFRACTION Dmax: 187.3 Å Quality: GOOD

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

PP2A scaffolding subunit

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 8–589 Chain B; UniProt 8–589 Fragment:UNP residues 8-589 Striatin-3 × 2 (Q13033) TME PROPANE × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;289 K;0.1M BIS-TRIS propane pH 9.0, 8.5% PEG20000 Resolution 3.33 Å R-free 0.249
2 Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain E; UniProt 8–589 Chain F; UniProt 8–589 Fragment:UNP residues 8-589 Striatin-3 × 2 (Q13033) TME PROPANE × 4 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;289 K;0.1M BIS-TRIS propane pH 9.0, 8.5% PEG20000 Resolution 3.33 Å R-free 0.249

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 1
Chains and sequence ranges Author chain A; PDBConstruct 6–587; UniProt 8–589 Author chain B; PDBConstruct 6–587; UniProt 8–589 Author chain E; PDBConstruct 6–587; UniProt 8–589 Author chain F; PDBConstruct 6–587; UniProt 8–589

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain C; UniProt 86–131 Chain D; UniProt 86–131 Fragment:UNP residues 86-131 PP2A scaffolding subunit × 2 (P30153) TME PROPANE × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;289 K;0.1M BIS-TRIS propane pH 9.0, 8.5% PEG20000 Resolution 3.33 Å R-free 0.249
2 Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain G; UniProt 86–131 Chain H; UniProt 86–131 Fragment:UNP residues 86-131 PP2A scaffolding subunit × 2 (P30153) TME PROPANE × 4 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;289 K;0.1M BIS-TRIS propane pH 9.0, 8.5% PEG20000 Resolution 3.33 Å R-free 0.249

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 3 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name STRN3_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain C; PDBConstruct 5–50; UniProt 86–131 Author chain D; PDBConstruct 5–50; UniProt 86–131 Author chain G; PDBConstruct 5–50; UniProt 86–131 Author chain H; PDBConstruct 5–50; UniProt 86–131

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 6iur

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6iur
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6iur
Deposition date deposition_date2018-11-30
Structure title titleA phosphatase complex STRN3-PP2Aa
Keywords keywordsPhosphatase, Complex, protein binding; PROTEIN BINDING
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier56.78
Radius of gyration Rg (electron density) rg_electron56.83
Forward intensity I(0) i01068920000.00
Molecular weight molecular_weight278380.0 kDa
Excluded volume excluded_volume351330 ų
Envelope volume envelope_volume569910 ų
Hydration-shell volume shell_volume86597 ų
Envelope diameter envelope_diameter193.7
Shell Rg shell_rg57.63
Envelope Rg envelope_rg54.25
Shape Rg shape_rg56.81
Total Rg total_rg56.94
Total atoms total_atoms19536
Residues n_residues2506
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 dmax187.3
Rg (real space) rg_real56.95
Rg uncertainty (real space) rg_real_error1.79
I(0) (real space) i0_real1.0690e+09
I(0) uncertainty (real space) i0_real_error2.1500e+07
Rg (reciprocal space) rg_reciprocal56.63
I(0) (reciprocal space) i0_reciprocal1068000000.0000
Solution quality estimate total_estimate0.8314
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary66.9
Skewness Skewness skewness0.433
Kurtosis Kurtosis kurtosis-0.178
Angular range angular_range— – 0.1400 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha43130000.0000
Real-space data points n_real_points29
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.868; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.999; Smooth: 0.202

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 8 domains

CATH v4.4 (8 domains)

Domain ID domain_id6iurA00
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_id6iurB00
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_id6iurC00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology5 — Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Homologous superfamily homologous superfamily300
Domain ID domain_id6iurD00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology5 — Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Homologous superfamily homologous superfamily300
Domain ID domain_id6iurE00
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_id6iurF00
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_id6iurG00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology5 — Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Homologous superfamily homologous superfamily300
Domain ID domain_id6iurH00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology5 — Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Homologous superfamily homologous superfamily300

8. Citations (1)

9. Files and Curves (10)