9fk5

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

Method: ELECTRON MICROSCOPY Dmax: 123.1 Å Quality: GOOD

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 TGF-beta receptor type-1 × 1 (P36897) TGF-beta receptor type-2 × 1 (P37173) Transforming growth factor beta receptor III × 1 (A0A0H3UK16) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.10 Å

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 13 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 B; PDBConstruct 1–112; UniProt 301–412

TGF-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 30–115 Not recorded Transforming growth factor beta-3 × 1 (P10600) Transforming growth factor beta-3 × 1 (P10600) TGF-beta receptor type-2 × 1 (P37173) Transforming growth factor beta receptor III × 1 (A0A0H3UK16) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.10 Å

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 63 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 1–87; UniProt 30–115

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 × 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 × 1 (P10600) TGF-beta receptor type-1 × 1 (P36897) Transforming growth factor beta receptor III × 1 (A0A0H3UK16) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.10 Å

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 4
Chains and sequence ranges Author chain D; PDBConstruct 2–113; UniProt 42–153

Transforming growth factor beta receptor III

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 × 1 (P10600) TGF-beta receptor type-1 × 1 (P36897) TGF-beta receptor type-2 × 1 (P37173) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.10 Å

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 6 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

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 9fk5

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9fk5
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9fk5
Deposition date deposition_date2024-06-02
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 methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier33.61
Radius of gyration Rg (electron density) rg_electron33.62
Forward intensity I(0) i0110992000.00
Molecular weight molecular_weight82378.0 kDa
Excluded volume excluded_volume102550 ų
Envelope volume envelope_volume138750 ų
Hydration-shell volume shell_volume37260 ų
Envelope diameter envelope_diameter130.3
Shell Rg shell_rg37.04
Envelope Rg envelope_rg33.42
Shape Rg shape_rg33.65
Total Rg total_rg33.78
Total atoms total_atoms5765
Residues n_residues735
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 dmax123.1
Rg (real space) rg_real33.89
Rg uncertainty (real space) rg_real_error1.49
I(0) (real space) i0_real1.1100e+08
I(0) uncertainty (real space) i0_real_error1.9760e+06
Rg (reciprocal space) rg_reciprocal33.72
I(0) (reciprocal space) i0_reciprocal111000000.0000
Solution quality estimate total_estimate0.8103
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary39.3
Skewness Skewness skewness0.649
Kurtosis Kurtosis kurtosis0.191
Angular range angular_range— – 0.2350 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha13320000.0000
Real-space data points n_real_points48
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.654; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.713; Smooth: 0.855

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

8. Citations (1)

9. Files and Curves (10)