6akl

Crystal structure of Striatin3 in complex with SIKE1 Coiled-coil domain

Method: X-RAY DIFFRACTION Dmax: 56.0 Å Quality: REASONABLE

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

Suppressor of IKBKE 1

Homo sapiens

UniProt Q9BRV8

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 72–121 Chain B; UniProt 72–121 Not recorded Striatin-3 × 1 (Q13033) 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

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.

2 other PDB entries and 2 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SIKE1_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 5–54; UniProt 72–121 Author chain B; PDBConstruct 5–54; UniProt 72–121

Striatin-3

OrganismNot specified

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain C; UniProt 165–190 Not recorded Suppressor of IKBKE 1 × 2 (Q9BRV8) 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

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
PDB entities 2
Chains and sequence ranges Author chain C; PDBConstruct 1–26; UniProt 165–190

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 6akl

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id6akl
Deposition date deposition_date2018-09-02
Structure title titleCrystal structure of Striatin3 in complex with SIKE1 Coiled-coil domain
Keywords keywordsCoiled-coil domain, heterotrimer, 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_guinier20.54
Radius of gyration Rg (electron density) rg_electron20.41
Forward intensity I(0) i04040380.00
Molecular weight molecular_weight13939.0 kDa
Excluded volume excluded_volume17293 ų
Envelope volume envelope_volume22304 ų
Hydration-shell volume shell_volume11016 ų
Envelope diameter envelope_diameter77.9
Shell Rg shell_rg23.60
Envelope Rg envelope_rg21.06
Shape Rg shape_rg20.32
Total Rg total_rg21.23
Total atoms total_atoms976
Residues n_residues118
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 dmax56.0
Rg (real space) rg_real19.12
Rg uncertainty (real space) rg_real_error0.13
I(0) (real space) i0_real3.8550e+06
I(0) uncertainty (real space) i0_real_error3.9210e+04
Rg (reciprocal space) rg_reciprocal20.87
I(0) (reciprocal space) i0_reciprocal4040000.0000
Solution quality estimate total_estimate0.6663
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks0
Primary peak position r_peak_primary
Skewness Skewness skewness0.445
Kurtosis Kurtosis kurtosis-0.565
Angular range angular_range— – 0.3850 −1
Current regularization parameter α current_alpha3.0430
Highest regularization parameter α highest_alpha422800.0000
Real-space data points n_real_points70
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.001; Oscil: 0.953; Stabil: 0.988; Sysdev: 0.000; Positv: 1.000; Valcen: 0.839; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)