9avt

Structure of TAB2 NZF domain bound to K6 / Lys6-linked diubiquitin

Method: X-RAY DIFFRACTION Dmax: 60.1 Å Quality: GOOD

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

Ubiquitin

Homo sapiens

UniProt P0CG47

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 1–76 Chain B; UniProt 1–76 Not recorded TGF-beta-activated kinase 1 and MAP3K7-binding protein 2 × 1 (Q9NYJ8) SO4 SULFATE ION × 4 DTT 2,3-DIHYDROXY-1,4-DITHIOBUTANE × 1 ZN ZINC ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;293 K;2.2 M ammonium sulphate Resolution 1.50 Å R-free 0.203

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.

278 other PDB entries and 429 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name UBB_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–76; UniProt 1–76 Author chain B; PDBConstruct 1–76; UniProt 1–76

TGF-beta-activated kinase 1 and MAP3K7-binding protein 2

Homo sapiens

UniProt Q9NYJ8

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 664–693 Not recorded Ubiquitin × 2 (P0CG47) SO4 SULFATE ION × 4 DTT 2,3-DIHYDROXY-1,4-DITHIOBUTANE × 1 ZN ZINC ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;293 K;2.2 M ammonium sulphate Resolution 1.50 Å R-free 0.203

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.

4 other PDB entries and 5 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name TAB2_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain C; PDBConstruct 1–30; UniProt 664–693

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 9avt

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id9avt
Deposition date deposition_date2024-03-04
最后修订 last_revision2024-07-31
Structure title titleStructure of TAB2 NZF domain bound to K6 / Lys6-linked diubiquitin
Keywords keywordsubiquitin binding domain, diubiquitin, Lys6-linkage, mitophagy, SIGNALING PROTEIN; SIGNALING PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier18.37
Radius of gyration Rg (electron density) rg_electron17.49
Forward intensity I(0) i07967980.00
Molecular weight molecular_weight20180.0 kDa
Excluded volume excluded_volume25094 ų
Envelope volume envelope_volume29845 ų
Hydration-shell volume shell_volume14901 ų
Envelope diameter envelope_diameter58.6
Shell Rg shell_rg22.55
Envelope Rg envelope_rg17.46
Shape Rg shape_rg17.50
Total Rg total_rg18.30
Total atoms total_atoms1403
Residues n_residues176
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 dmax60.1
Rg (real space) rg_real18.35
Rg uncertainty (real space) rg_real_error0.33
I(0) (real space) i0_real7.9680e+06
I(0) uncertainty (real space) i0_real_error9.4580e+04
Rg (reciprocal space) rg_reciprocal18.35
I(0) (reciprocal space) i0_reciprocal7968000.0000
Solution quality estimate total_estimate0.8912
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary20.3
Skewness Skewness skewness0.325
Kurtosis Kurtosis kurtosis-0.332
Angular range angular_range— – 0.4350 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha1463000.0000
Real-space data points n_real_points75
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.864; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.998; Smooth: 0.992

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

8. Citations (1)

9. Files and Curves (10)