SAXSdb — 4n6j

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

Striatin-3

Homo sapiens

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 homooligomer Homooligomer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain A； UniProt 86–131 Chain B； UniProt 86–131	Fragment：UNP residues 86-131 Mutation：F99M, Y123M Non-standard monomer：Yes (specific site not provided by mmCIF)	No other associated polymer	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, SITTING DROP；pH 6.5；289 K；0.1M Bis-Tris pH 6.5, 0.2M MgCl2, 23% PEG3350, VAPOR DIFFUSION, SITTING DROP, temperature 289K	Resolution 2.00 Å R-free 0.252

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.

Other PDB	Difference from Current Entry 4N6J	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
6AKL Crystal structure of Striatin3 in complex with SIKE1 Coiled-coil domain Deposited 2018-09-02	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric	Chain C 165–190（26 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；289 K；35% (v/v) MPD; 0.1 M imidazole pH 7.5	Resolution 1.75 Å R-free 0.213
6IUR A phosphatase complex STRN3-PP2Aa Deposited 2018-11-30	Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain C 86–131（46 aa） Fragment：UNP residues 86-131 Chain D 86–131（46 aa） Fragment：UNP residues 86-131	Not recorded	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
6IUR A phosphatase complex STRN3-PP2Aa Deposited 2018-11-30	Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain G 86–131（46 aa） Fragment：UNP residues 86-131 Chain H 86–131（46 aa） Fragment：UNP residues 86-131	Not recorded	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
7K36 Cryo-EM structure of STRIPAK complex Deposited 2020-09-10	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 9 PDB declaration: nonameric	Chain B 1–713（713 aa） Chain D 1–713（713 aa） Chain E 1–713（713 aa） Chain F 1–713（713 aa） Chain G 1–713（713 aa）	Not recorded	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

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	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 5–50； UniProt 86–131 Author chain B； 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.

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2. Structure Basics 2. Structure Basics

Entry ID entry_id	4n6j
Deposition date deposition_date	2013-10-13
Structure title title	Crystal structure of human Striatin-3 coiled coil domain
Keywords keywords	WD40, scaffolding protein, PP2A, CCM3, CaM, CaV, Rassf., SIGNALING PROTEIN; SIGNALING PROTEIN
Experimental Method method	X-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier	21.72 Å
Radius of gyration Rg (electron density) rg_electron	21.71 Å
Forward intensity I(0) i0	3181800.00
Molecular weight molecular_weight	11748.0 kDa
Excluded volume excluded_volume	14210 Å³
Envelope volume envelope_volume	18699 Å³
Hydration-shell volume shell_volume	9150 Å³
Envelope diameter envelope_diameter	78.0 Å
Shell Rg shell_rg	23.74 Å
Envelope Rg envelope_rg	22.08 Å
Shape Rg shape_rg	21.61 Å
Total Rg total_rg	22.32 Å
Total atoms total_atoms	790
Residues n_residues	88
Spherical-harmonic order n_harmonics	20
q range q_range	— – 0.5000 Å⁻¹
Data points n_points	101
Shell type shell_type	directional
Solvent electron density solvent_density	0.3340 e/Å³
Shell contrast contrast_shell	0.0300 e/Å³
CRYSOL version crysol_version	4.1.3

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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax	79.2 Å
Rg (real space) rg_real	22.29 Å
Rg uncertainty (real space) rg_real_error	0.91 Å
I(0) (real space) i0_real	3.1820e+06
I(0) uncertainty (real space) i0_real_error	4.7530e+04
Rg (reciprocal space) rg_reciprocal	22.19 Å
I(0) (reciprocal space) i0_reciprocal	3182000.0000
Solution quality estimate total_estimate	0.7071
Solution quality rating solution_quality	REASONABLE a REASONABLE solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	15.4 Å
Skewness Skewness skewness	0.659
Kurtosis Kurtosis kurtosis	-0.343
Angular range angular_range	— – 0.3650 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	310500.0000
Real-space data points n_real_points	68
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.386; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.046; Smooth: 0.985

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (2)

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7. Fold Classification (SCOP + CATH) 2 domains

CATH v4.4 (2 domains)

Domain ID domain_id	4n6jA00
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	5 — Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Homologous superfamily homologous superfamily	300 —

Domain ID domain_id	4n6jB00
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	5 — Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Homologous superfamily homologous superfamily	300 —

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8. Citations (1)

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Unit-cell length a length_a	34.064 Å
Unit-cell length b length_b	34.064 Å
Unit-cell length c length_c	161.388 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	90.00 °
Unit-cell angle γ angle_gamma	120.00 °
Molecules per unit cell Z z_pdb	12

Space group space_group	P 32 2 1
Space-group number int_tables_number	154
Crystal system crystal_system	—

Resolution resolution	2.001 Å
Low-resolution limit resolution_low	29.500 Å
R factor r_factor	0.2085
R_work r_work	0.2035
R_free r_free	0.2521

Description description	Striatin-3
Molecular weight formula_weight	6156.6 kDa
Mutation mutation	F99M, Y123M
Source method src_method	man
Copy count entity_count	2

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B
Atom count atom_count	904

Crystal structure of human Striatin-3 coiled coil domain

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

Striatin-3

State in the Current Structure

Other States of the Same Protein in the Database

SAXS scattering curve SAXS Profile

P(r) Distance Distribution P(r) Distribution

2. Structure Basics 2. Structure Basics

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

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

5. Crystallography and Experiment 5. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

Diffraction experiment Diffraction

6. Entities and Polymers Entities & Polymers (2)

Entity 1 Entity 1 polymer

Polymer Polymer

来源 Source

Entity 2 Entity 2 water

7. Fold Classification (SCOP + CATH) 2 domains

CATH v4.4 (2 domains)

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)

来源生物 organism	Homo sapiens
通用名 common_name	human
NCBI Class编号 ncbi_taxonomy_id	9606
宿主生物 host_organism	Escherichia coli

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	114

fit	/app/data/saxs_computation/n6/4n6j/4n6j.fit
pddf	/app/data/pr_computation/n6/4n6j/4n6j.pr.out
profile	/app/data/saxs_computation/n6/4n6j/4n6j.dat