9b9f

Zebrafish Betaglycan Orphan Domain (zfBGo) in complex with TGF-B3 and extracellular domains of TGFBRI and TGFBRII

Method: X-RAY DIFFRACTION Dmax: 193.6 Å Quality: REASONABLE

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

Transforming growth factor beta-3

Homo sapiens

UniProt P10600

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 × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain A; UniProt 301–412 Chain B; UniProt 301–412 Mutation:R325E,Y390A,R394E Transforming growth factor beta receptor type-1 × 1 (P36897) Transforming growth factor beta receptor type-2 × 1 (P37173) Transforming growth factor beta receptor type-3 × 1 (A0A0H3UK16) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;298 K;0.2 M lithium sulfate, 0.1 M tris pH 8.5, 30 %(w/v) polyethylene glycol 4000 Resolution 3.00 Å R-free 0.278
2 Protein heterocomplex Heteromer Protein × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain F; UniProt 301–412 Chain G; UniProt 301–412 Mutation:R325E,Y390A,R394E Transforming growth factor beta receptor type-1 × 1 (P36897) Transforming growth factor beta receptor type-2 × 1 (P37173) Transforming growth factor beta receptor type-3 × 1 (A0A0H3UK16) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;298 K;0.2 M lithium sulfate, 0.1 M tris pH 8.5, 30 %(w/v) polyethylene glycol 4000 Resolution 3.00 Å R-free 0.278

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.

10 other PDB entries and 12 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name TGFB3_HUMAN
Isoform
PDB entities 1, 2
Chains and sequence ranges Author chain A; PDBConstruct 1–112; UniProt 301–412 Author chain F; PDBConstruct 1–112; UniProt 301–412 Author chain B; PDBConstruct 1–112; UniProt 301–412 Author chain G; PDBConstruct 1–112; UniProt 301–412

Transforming growth factor beta receptor type-1

Homo sapiens

UniProt P36897

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 × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain C; UniProt 31–115 Not recorded Transforming growth factor beta-3 × 1 (P10600) Transforming growth factor beta-3 triple mutant × 1 (P10600) Transforming growth factor beta receptor type-2 × 1 (P37173) Transforming growth factor beta receptor type-3 × 1 (A0A0H3UK16) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;298 K;0.2 M lithium sulfate, 0.1 M tris pH 8.5, 30 %(w/v) polyethylene glycol 4000 Resolution 3.00 Å R-free 0.278
2 Protein heterocomplex Heteromer Protein × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain H; UniProt 31–115 Not recorded Transforming growth factor beta-3 × 1 (P10600) Transforming growth factor beta-3 triple mutant × 1 (P10600) Transforming growth factor beta receptor type-2 × 1 (P37173) Transforming growth factor beta receptor type-3 × 1 (A0A0H3UK16) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;298 K;0.2 M lithium sulfate, 0.1 M tris pH 8.5, 30 %(w/v) polyethylene glycol 4000 Resolution 3.00 Å R-free 0.278

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.

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

View Construct and Data Evidence
UniProt name TGFR1_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 3–87; UniProt 31–115 Author chain H; PDBConstruct 3–87; UniProt 31–115

Transforming growth factor 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 × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain D; UniProt 42–153 Not recorded Transforming growth factor beta-3 × 1 (P10600) Transforming growth factor beta-3 triple mutant × 1 (P10600) Transforming growth factor beta receptor type-1 × 1 (P36897) Transforming growth factor beta receptor type-3 × 1 (A0A0H3UK16) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;298 K;0.2 M lithium sulfate, 0.1 M tris pH 8.5, 30 %(w/v) polyethylene glycol 4000 Resolution 3.00 Å R-free 0.278
2 Protein heterocomplex Heteromer Protein × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain I; UniProt 42–153 Not recorded Transforming growth factor beta-3 × 1 (P10600) Transforming growth factor beta-3 triple mutant × 1 (P10600) Transforming growth factor beta receptor type-1 × 1 (P36897) Transforming growth factor beta receptor type-3 × 1 (A0A0H3UK16) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;298 K;0.2 M lithium sulfate, 0.1 M tris pH 8.5, 30 %(w/v) polyethylene glycol 4000 Resolution 3.00 Å R-free 0.278

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 23 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name TGFR2_HUMAN
Isoform
PDB entities 4
Chains and sequence ranges Author chain D; PDBConstruct 2–113; UniProt 42–153 Author chain I; PDBConstruct 2–113; UniProt 42–153

Transforming growth factor beta receptor type-3

Danio rerio

UniProt A0A0H3UK16

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 × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain E; UniProt 29–359 Mutation:C150G,C277G Transforming growth factor beta-3 × 1 (P10600) Transforming growth factor beta-3 triple mutant × 1 (P10600) Transforming growth factor beta receptor type-1 × 1 (P36897) Transforming growth factor beta receptor type-2 × 1 (P37173) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;298 K;0.2 M lithium sulfate, 0.1 M tris pH 8.5, 30 %(w/v) polyethylene glycol 4000 Resolution 3.00 Å R-free 0.278
2 Protein heterocomplex Heteromer Protein × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain J; UniProt 29–359 Mutation:C150G,C277G Transforming growth factor beta-3 × 1 (P10600) Transforming growth factor beta-3 triple mutant × 1 (P10600) Transforming growth factor beta receptor type-1 × 1 (P36897) Transforming growth factor beta receptor type-2 × 1 (P37173) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;298 K;0.2 M lithium sulfate, 0.1 M tris pH 8.5, 30 %(w/v) polyethylene glycol 4000 Resolution 3.00 Å R-free 0.278

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 A0A0H3UK16_DANRE
Isoform
PDB entities 5
Chains and sequence ranges Author chain E; PDBConstruct 2–332; UniProt 29–359 Author chain J; PDBConstruct 2–332; UniProt 29–359

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 9b9f

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9b9f
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9b9f
Deposition date deposition_date2024-04-02
最后修订 last_revision2025-03-12
Structure title titleZebrafish Betaglycan Orphan Domain (zfBGo) in complex with TGF-B3 and extracellular domains of TGFBRI and TGFBRII
Keywords keywordsComplex, Betaglycan, TGFBR3, TGFb, TGFBR1, TGFBR2, MEMBRANE PROTEIN; MEMBRANE PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier54.20
Radius of gyration Rg (electron density) rg_electron55.97
Forward intensity I(0) i0374588000.00
Molecular weight molecular_weight158320.0 kDa
Excluded volume excluded_volume197250 ų
Envelope volume envelope_volume294240 ų
Hydration-shell volume shell_volume50008 ų
Envelope diameter envelope_diameter208.3
Shell Rg shell_rg48.27
Envelope Rg envelope_rg55.68
Shape Rg shape_rg56.11
Total Rg total_rg55.21
Total atoms total_atoms11078
Residues n_residues1408
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 dmax193.6
Rg (real space) rg_real55.14
Rg uncertainty (real space) rg_real_error2.75
I(0) (real space) i0_real3.7460e+08
I(0) uncertainty (real space) i0_real_error7.9570e+06
Rg (reciprocal space) rg_reciprocal53.41
I(0) (reciprocal space) i0_reciprocal373700000.0000
Solution quality estimate total_estimate0.6874
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary40.0
Skewness Skewness skewness0.671
Kurtosis Kurtosis kurtosis-0.302
Angular range angular_range— – 0.1450 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha23200000.0000
Real-space data points n_real_points30
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.341; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.417; Smooth: 0.493

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

8. Citations (1)

9. Files and Curves (10)