9e9g

Heligmosomoides polygyrus TGF-beta Mimic 6 Domain 3 (TGM6-D3) Bound to Human TGF-beta Type II Receptor Extracellular Domain

Method: X-RAY DIFFRACTION Dmax: 65.6 Å Quality: GOOD

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

TGF-beta receptor type-2

Homo sapiens

UniProt P37173

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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 38–154 Fragment:UNP residues 38-154 Transforming growth factor beta mimic 6 × 1 (A0A2P1IQ80) GOL GLYCEROL × 8 CL CHLORIDE ION × 2 NA SODIUM ION × 5 CAC CACODYLATE ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.5;298 K;0.1 M sodium cacodylate, 25% w/v PEG4000, pH 6.5 Resolution 1.40 Å R-free 0.182

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.

21 other PDB entries and 24 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name TGFR2_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 2–118; UniProt 38–154

Transforming growth factor beta mimic 6

Heligmosomoides polygyrus

UniProt A0A2P1IQ80

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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 15–102 Fragment:Domain 3, UNP residues 15-102 TGF-beta receptor type-2 × 1 (P37173) GOL GLYCEROL × 8 CL CHLORIDE ION × 2 NA SODIUM ION × 5 CAC CACODYLATE ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.5;298 K;0.1 M sodium cacodylate, 25% w/v PEG4000, pH 6.5 Resolution 1.40 Å R-free 0.182

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.

1 other PDB entries and 2 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name A0A2P1IQ80_HELBE
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 5–92; UniProt 15–102

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 9e9g

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9e9g
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9e9g
Deposition date deposition_date2024-11-08
Structure title titleHeligmosomoides polygyrus TGF-beta Mimic 6 Domain 3 (TGM6-D3) Bound to Human TGF-beta Type II Receptor Extracellular Domain
Keywords keywordsInhibitor, Complex, TGF-beta mimic, HpTGM, TGM6, TGM6-D3, TGF-beta, TbRII, fibroblasts, IMMUNOSUPPRESSANT; IMMUNOSUPPRESSANT
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier19.23
Radius of gyration Rg (electron density) rg_electron18.78
Forward intensity I(0) i010769000.00
Molecular weight molecular_weight23335.0 kDa
Excluded volume excluded_volume28581 ų
Envelope volume envelope_volume34077 ų
Hydration-shell volume shell_volume15810 ų
Envelope diameter envelope_diameter64.6
Shell Rg shell_rg24.13
Envelope Rg envelope_rg19.16
Shape Rg shape_rg18.84
Total Rg total_rg19.39
Total atoms total_atoms3104
Residues n_residues193
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 dmax65.6
Rg (real space) rg_real19.28
Rg uncertainty (real space) rg_real_error0.60
I(0) (real space) i0_real1.0770e+07
I(0) uncertainty (real space) i0_real_error1.6140e+05
Rg (reciprocal space) rg_reciprocal19.28
I(0) (reciprocal space) i0_reciprocal10770000.0000
Solution quality estimate total_estimate0.8664
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary20.0
Skewness Skewness skewness0.397
Kurtosis Kurtosis kurtosis-0.415
Angular range angular_range— – 0.4150 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha2919000.0000
Real-space data points n_real_points73
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.799; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.889; Smooth: 0.976

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (7)

8. Citations (1)

9. Files and Curves (10)