7t8j

The ubiquitin-associated domain of human thirty-eight negative kinase-1 flexibly fused to the 1TEL crystallization chaperone via a GSGG linker

Method: X-RAY DIFFRACTION Dmax: 69.3 Å Quality: GOOD

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 47–121 Mutation:R80S,V112E,C610A,C644A CL CHLORIDE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7;298 K;1.2 uL of 1 mg/mL protein in 50 mM Tris pH 8.8, 200 mM KCl combined with 1.2 uL of 100 mM Bis-tris-propane, 2.5 M Ammonium Nitrate Resolution 1.89 Å R-free 0.235

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 64 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 2–76; UniProt 47–121

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 Mutation:R80S,V112E,C610A,C644A CL CHLORIDE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7;298 K;1.2 uL of 1 mg/mL protein in 50 mM Tris pH 8.8, 200 mM KCl combined with 1.2 uL of 100 mM Bis-tris-propane, 2.5 M Ammonium Nitrate Resolution 1.89 Å R-free 0.235

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 13 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 81–157; 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 7t8j

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7t8j
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7t8j
Deposition date deposition_date2021-12-16
Structure title titleThe ubiquitin-associated domain of human thirty-eight negative kinase-1 flexibly fused to the 1TEL crystallization chaperone via a GSGG linker
Keywords keywordsProtein polymer, Ubiquitin-associated domain, Helix bundle, Chimera, ONCOPROTEIN; ONCOPROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier20.21
Radius of gyration Rg (electron density) rg_electron19.41
Forward intensity I(0) i04444680.00
Molecular weight molecular_weight15429.0 kDa
Excluded volume excluded_volume19369 ų
Envelope volume envelope_volume24209 ų
Hydration-shell volume shell_volume11730 ų
Envelope diameter envelope_diameter67.0
Shell Rg shell_rg23.44
Envelope Rg envelope_rg19.66
Shape Rg shape_rg19.46
Total Rg total_rg19.97
Total atoms total_atoms1096
Residues n_residues147
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 dmax69.3
Rg (real space) rg_real20.42
Rg uncertainty (real space) rg_real_error0.71
I(0) (real space) i0_real4.4450e+06
I(0) uncertainty (real space) i0_real_error6.9630e+04
Rg (reciprocal space) rg_reciprocal20.38
I(0) (reciprocal space) i0_reciprocal4445000.0000
Solution quality estimate total_estimate0.7957
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary17.8
Skewness Skewness skewness0.525
Kurtosis Kurtosis kurtosis-0.457
Angular range angular_range— – 0.3950 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha1027000.0000
Real-space data points n_real_points71
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.579; Stabil: 0.996; Sysdev: 1.000; Positv: 1.000; Valcen: 0.639; Smooth: 0.979

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 1 domains

CATH v4.4 (1 domains)

Domain ID domain_id7t8jA01
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology150 — DNA polymerase; domain 1
Homologous superfamily homologous superfamily50 — Transcription Factor, Ets-1

8. Citations (1)

9. Files and Curves (10)