9zvu

The ubiquitin-associated domain of human thirty-eight negative kinase-1 rigidly fused to a double trigger variant of the 1TEL crystallization chaperone, alternate crystal form

Method: X-RAY DIFFRACTION Dmax: 73.1 Å Quality: EXCELLENT

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

Transcription factor ETV6,Non-receptor tyrosine-protein kinase TNK1

Homo sapiens

UniProt P41212

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 47–122 Fragment:TNK1 UBA domain,TNK1 UBA domain Mutation:R80S,L96E,V112E,L591V,C610A,C644A TLA L(+)-TARTARIC ACID × 4 NA SODIUM ION × 4 SO4 SULFATE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7;298 K;0.2M Sodium Tartrate, 16% PEG 3350 Monodisperse Resolution 1.96 Å R-free 0.247
2 Insufficient information Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain B; UniProt 47–122 Fragment:TNK1 UBA domain,TNK1 UBA domain Mutation:R80S,L96E,V112E,L591V,C610A,C644A TLA L(+)-TARTARIC ACID × 3 NA SODIUM ION × 4 SO4 SULFATE ION × 2 TAR D(-)-TARTARIC ACID × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7;298 K;0.2M Sodium Tartrate, 16% PEG 3350 Monodisperse Resolution 1.96 Å R-free 0.247

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.

40 other PDB entries and 63 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ETV6_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 13–88; UniProt 47–122 Author chain B; PDBConstruct 13–88; UniProt 47–122

Transcription factor ETV6,Non-receptor tyrosine-protein kinase TNK1

Homo sapiens

UniProt Q13470

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 590–666 Fragment:TNK1 UBA domain,TNK1 UBA domain Mutation:R80S,L96E,V112E,L591V,C610A,C644A TLA L(+)-TARTARIC ACID × 4 NA SODIUM ION × 4 SO4 SULFATE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7;298 K;0.2M Sodium Tartrate, 16% PEG 3350 Monodisperse Resolution 1.96 Å R-free 0.247
2 Insufficient information Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain B; UniProt 590–666 Fragment:TNK1 UBA domain,TNK1 UBA domain Mutation:R80S,L96E,V112E,L591V,C610A,C644A TLA L(+)-TARTARIC ACID × 3 NA SODIUM ION × 4 SO4 SULFATE ION × 2 TAR D(-)-TARTARIC ACID × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7;298 K;0.2M Sodium Tartrate, 16% PEG 3350 Monodisperse Resolution 1.96 Å R-free 0.247

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 12 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name TNK1_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 89–165; UniProt 590–666 Author chain B; PDBConstruct 89–165; UniProt 590–666

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 9zvu

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id9zvu
Deposition date deposition_date2025-12-30
最后修订 last_revision2026-03-04
Structure title titleThe ubiquitin-associated domain of human thirty-eight negative kinase-1 rigidly fused to a double trigger variant of the 1TEL crystallization chaperone, alternate crystal form
Keywords keywords;Sterile Alpha Motif (SAM) of Human Translocation ETS Leukemia (TEL), protein crystallization chaperone, TELSAM, ETV6, TRANSCRIPTION, 1TEL Crystallization Chaperone, ONCOPROTEIN, TNK1, UBA, Ubiquitin-Associated Domain, Thirty-eight Negative Kinase-1 ;; ONCOPROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier23.40
Radius of gyration Rg (electron density) rg_electron22.38
Forward intensity I(0) i021095400.00
Molecular weight molecular_weight33746.0 kDa
Excluded volume excluded_volume41727 ų
Envelope volume envelope_volume52661 ų
Hydration-shell volume shell_volume20534 ų
Envelope diameter envelope_diameter74.6
Shell Rg shell_rg28.19
Envelope Rg envelope_rg22.31
Shape Rg shape_rg22.36
Total Rg total_rg23.25
Total atoms total_atoms4523
Residues n_residues306
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 dmax73.1
Rg (real space) rg_real23.35
Rg uncertainty (real space) rg_real_error0.49
I(0) (real space) i0_real2.1100e+07
I(0) uncertainty (real space) i0_real_error2.5910e+05
Rg (reciprocal space) rg_reciprocal23.36
I(0) (reciprocal space) i0_reciprocal21100000.0000
Solution quality estimate total_estimate0.9140
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary29.2
Skewness Skewness skewness0.210
Kurtosis Kurtosis kurtosis-0.557
Angular range angular_range— – 0.3400 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha3832000.0000
Real-space data points n_real_points66
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.962; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.995; Smooth: 0.998

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

8. Citations (1)

9. Files and Curves (10)