7tcy

The ubiquitin-associated domain of human thirty-eight negative kinase I

Method: X-RAY DIFFRACTION Dmax: 65.7 Å Quality: GOOD

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

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 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 589–666 Fragment:UBA domain (UNP residues 589-666) Mutation:P589G, C610A, C644A FMT FORMIC ACID × 3 PO4 PHOSPHATE ION × 1 MG MAGNESIUM ION × 1 CL CHLORIDE ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6.8;298 K;100 mM Bis-Tris, pH 6.8, 100 mM magnesium formate Resolution 1.54 Å R-free 0.214
2 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain B; UniProt 589–666 Fragment:UBA domain (UNP residues 589-666) Mutation:P589G, C610A, C644A FMT FORMIC ACID × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6.8;298 K;100 mM Bis-Tris, pH 6.8, 100 mM magnesium formate Resolution 1.54 Å R-free 0.214

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 1–78; UniProt 589–666 Author chain B; PDBConstruct 1–78; UniProt 589–666

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 7tcy

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id7tcy
Deposition date deposition_date2021-12-29
Structure title titleThe ubiquitin-associated domain of human thirty-eight negative kinase I
Keywords keywordsKinase, Ubiquitin-associated, UBA, ONCOPROTEIN, TRANSFERASE; TRANSFERASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier17.78
Radius of gyration Rg (electron density) rg_electron16.80
Forward intensity I(0) i06233610.00
Molecular weight molecular_weight17344.0 kDa
Excluded volume excluded_volume21402 ų
Envelope volume envelope_volume25733 ų
Hydration-shell volume shell_volume13500 ų
Envelope diameter envelope_diameter66.0
Shell Rg shell_rg21.86
Envelope Rg envelope_rg17.08
Shape Rg shape_rg16.78
Total Rg total_rg17.72
Total atoms total_atoms2401
Residues n_residues154
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 dmax65.7
Rg (real space) rg_real17.76
Rg uncertainty (real space) rg_real_error0.76
I(0) (real space) i0_real6.2340e+06
I(0) uncertainty (real space) i0_real_error1.0220e+05
Rg (reciprocal space) rg_reciprocal17.76
I(0) (reciprocal space) i0_reciprocal6234000.0000
Solution quality estimate total_estimate0.8274
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary64.8
Skewness Skewness skewness0.310
Kurtosis Kurtosis kurtosis-0.193
Angular range angular_range— – 0.4450 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha1875000.0000
Real-space data points n_real_points75
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.619; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.909; Smooth: 0.989

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

8. Citations (1)

9. Files and Curves (10)