9q9e

Crystal structure of a TELSAM-SUMO1 fusion protein

Method: X-RAY DIFFRACTION Dmax: 100.1 Å Quality: GOOD

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

Transcription factor ETV6,Small ubiquitin-related modifier 1

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 47–123 Mutation:V73E 1PE PENTAETHYLENE GLYCOL × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;293 K;Na-phosphate/citric acid pH4.2, PEG600 Resolution 2.05 Å R-free 0.231
2 Insufficient information Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain B; UniProt 47–123 Mutation:V73E PO4 PHOSPHATE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;293 K;Na-phosphate/citric acid pH4.2, PEG600 Resolution 2.05 Å R-free 0.231
3 Insufficient information Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain C; UniProt 47–123 Mutation:V73E No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;293 K;Na-phosphate/citric acid pH4.2, PEG600 Resolution 2.05 Å R-free 0.231

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 62 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 8–84; UniProt 47–123 Author chain B; PDBConstruct 8–84; UniProt 47–123 Author chain C; PDBConstruct 8–84; UniProt 47–123

Transcription factor ETV6,Small ubiquitin-related modifier 1

Homo sapiens

UniProt P63165

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 18–97 Mutation:V73E 1PE PENTAETHYLENE GLYCOL × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;293 K;Na-phosphate/citric acid pH4.2, PEG600 Resolution 2.05 Å R-free 0.231
2 Insufficient information Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain B; UniProt 18–97 Mutation:V73E PO4 PHOSPHATE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;293 K;Na-phosphate/citric acid pH4.2, PEG600 Resolution 2.05 Å R-free 0.231
3 Insufficient information Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain C; UniProt 18–97 Mutation:V73E No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;293 K;Na-phosphate/citric acid pH4.2, PEG600 Resolution 2.05 Å R-free 0.231

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.

62 other PDB entries and 91 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SUMO1_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 88–167; UniProt 18–97 Author chain B; PDBConstruct 88–167; UniProt 18–97 Author chain C; PDBConstruct 88–167; UniProt 18–97

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 9q9e

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9q9e
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9q9e
Deposition date deposition_date2025-02-26
Structure title titleCrystal structure of a TELSAM-SUMO1 fusion protein
Keywords keywordsSUMOylation, fusion protein-assisted crystallisation, TELSAM domain, SUMO1 protein, 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_guinier32.36
Radius of gyration Rg (electron density) rg_electron31.17
Forward intensity I(0) i040342300.00
Molecular weight molecular_weight48850.0 kDa
Excluded volume excluded_volume60666 ų
Envelope volume envelope_volume89702 ų
Hydration-shell volume shell_volume25254 ų
Envelope diameter envelope_diameter106.8
Shell Rg shell_rg36.44
Envelope Rg envelope_rg30.58
Shape Rg shape_rg31.20
Total Rg total_rg31.61
Total atoms total_atoms3456
Residues n_residues459
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 dmax100.1
Rg (real space) rg_real32.31
Rg uncertainty (real space) rg_real_error0.79
I(0) (real space) i0_real4.0340e+07
I(0) uncertainty (real space) i0_real_error5.7100e+05
Rg (reciprocal space) rg_reciprocal32.34
I(0) (reciprocal space) i0_reciprocal40340000.0000
Solution quality estimate total_estimate0.8794
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary45.0
Skewness Skewness skewness0.139
Kurtosis Kurtosis kurtosis-0.510
Angular range angular_range— – 0.2450 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha2962000.0000
Real-space data points n_real_points50
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.861; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.974; Smooth: 0.873

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)