3kfd

Ternary complex of TGF-b1 reveals isoform-specific ligand recognition and receptor recruitment in the superfamily

Method: X-RAY DIFFRACTION Dmax: 151.0 Å Quality: GOOD

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

Transforming growth factor beta-1

Homo sapiens

UniProt P01137

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 × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain A; UniProt 279–390 Chain B; UniProt 279–390 Not recorded TGF-beta receptor type-2 × 2 (P37173) TGF-beta receptor type-1 × 2 (P36897) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;pH 7;298 K;8-15% Peg 4000-8000, pH 7.0, VAPOR DIFFUSION, temperature 298K Resolution 3.00 Å R-free 0.268
2 Protein heterocomplex Heteromer Protein × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain C; UniProt 279–390 Chain D; UniProt 279–390 Not recorded TGF-beta receptor type-2 × 2 (P37173) TGF-beta receptor type-1 × 2 (P36897) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;pH 7;298 K;8-15% Peg 4000-8000, pH 7.0, VAPOR DIFFUSION, temperature 298K Resolution 3.00 Å R-free 0.268
3 Protein heterocomplex Heteromer Protein × 12 PDB declaration: dodecameric(12) Consistent with protein copy count Chain A; UniProt 279–390 Chain B; UniProt 279–390 Chain C; UniProt 279–390 Chain D; UniProt 279–390 Not recorded TGF-beta receptor type-2 × 4 (P37173) TGF-beta receptor type-1 × 4 (P36897) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;pH 7;298 K;8-15% Peg 4000-8000, pH 7.0, VAPOR DIFFUSION, temperature 298K Resolution 3.00 Å R-free 0.268

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.

17 other PDB entries and 19 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name TGFB1_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–112; UniProt 279–390 Author chain B; PDBConstruct 1–112; UniProt 279–390 Author chain C; PDBConstruct 1–112; UniProt 279–390 Author chain D; PDBConstruct 1–112; UniProt 279–390

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 × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain E; UniProt 38–153 Chain F; UniProt 38–153 Fragment:extracellular domain Transforming growth factor beta-1 × 2 (P01137) TGF-beta receptor type-1 × 2 (P36897) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;pH 7;298 K;8-15% Peg 4000-8000, pH 7.0, VAPOR DIFFUSION, temperature 298K Resolution 3.00 Å R-free 0.268
2 Protein heterocomplex Heteromer Protein × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain G; UniProt 38–153 Chain H; UniProt 38–153 Fragment:extracellular domain Transforming growth factor beta-1 × 2 (P01137) TGF-beta receptor type-1 × 2 (P36897) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;pH 7;298 K;8-15% Peg 4000-8000, pH 7.0, VAPOR DIFFUSION, temperature 298K Resolution 3.00 Å R-free 0.268
3 Protein heterocomplex Heteromer Protein × 12 PDB declaration: dodecameric(12) Consistent with protein copy count Chain E; UniProt 38–153 Chain F; UniProt 38–153 Chain G; UniProt 38–153 Chain H; UniProt 38–153 Fragment:extracellular domain Transforming growth factor beta-1 × 4 (P01137) TGF-beta receptor type-1 × 4 (P36897) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;pH 7;298 K;8-15% Peg 4000-8000, pH 7.0, VAPOR DIFFUSION, temperature 298K Resolution 3.00 Å R-free 0.268

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 22 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name TGFR2_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain E; PDBConstruct 1–116; UniProt 38–153 Author chain F; PDBConstruct 1–116; UniProt 38–153 Author chain G; PDBConstruct 1–116; UniProt 38–153 Author chain H; PDBConstruct 1–116; UniProt 38–153

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 × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain I; UniProt 31–115 Chain J; UniProt 31–115 Fragment:extracellular domain Transforming growth factor beta-1 × 2 (P01137) TGF-beta receptor type-2 × 2 (P37173) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;pH 7;298 K;8-15% Peg 4000-8000, pH 7.0, VAPOR DIFFUSION, temperature 298K Resolution 3.00 Å R-free 0.268
2 Protein heterocomplex Heteromer Protein × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain K; UniProt 31–115 Chain L; UniProt 31–115 Fragment:extracellular domain Transforming growth factor beta-1 × 2 (P01137) TGF-beta receptor type-2 × 2 (P37173) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;pH 7;298 K;8-15% Peg 4000-8000, pH 7.0, VAPOR DIFFUSION, temperature 298K Resolution 3.00 Å R-free 0.268
3 Protein heterocomplex Heteromer Protein × 12 PDB declaration: dodecameric(12) Consistent with protein copy count Chain I; UniProt 31–115 Chain J; UniProt 31–115 Chain K; UniProt 31–115 Chain L; UniProt 31–115 Fragment:extracellular domain Transforming growth factor beta-1 × 4 (P01137) TGF-beta receptor type-2 × 4 (P37173) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;pH 7;298 K;8-15% Peg 4000-8000, pH 7.0, VAPOR DIFFUSION, temperature 298K Resolution 3.00 Å R-free 0.268

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 61 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 I; PDBConstruct 1–85; UniProt 31–115 Author chain J; PDBConstruct 1–85; UniProt 31–115 Author chain K; PDBConstruct 1–85; UniProt 31–115 Author chain L; PDBConstruct 1–85; UniProt 31–115

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 3kfd

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 3kfd
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2. Structure Basics 2. Structure Basics

Entry ID entry_id3kfd
Deposition date deposition_date2009-10-27
Structure title titleTernary complex of TGF-b1 reveals isoform-specific ligand recognition and receptor recruitment in the superfamily
Keywords keywords;TGF-beta, TGF-b1, TGF-beta receptor type-1, TGF-beta receptor type-2, TbRII, TbRI, Growth factor, Receptor, Serine/threonine-protein kinase, CYTOKINE-CYTOKINE RECEPTOR complex ;; CYTOKINE/CYTOKINE RECEPTOR
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier41.94
Radius of gyration Rg (electron density) rg_electron42.05
Forward intensity I(0) i0271462000.00
Molecular weight molecular_weight130350.0 kDa
Excluded volume excluded_volume161370 ų
Envelope volume envelope_volume228380 ų
Hydration-shell volume shell_volume47627 ų
Envelope diameter envelope_diameter160.0
Shell Rg shell_rg44.62
Envelope Rg envelope_rg41.84
Shape Rg shape_rg42.07
Total Rg total_rg42.09
Total atoms total_atoms9058
Residues n_residues1149
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 dmax151.0
Rg (real space) rg_real42.12
Rg uncertainty (real space) rg_real_error2.12
I(0) (real space) i0_real2.7150e+08
I(0) uncertainty (real space) i0_real_error5.7120e+06
Rg (reciprocal space) rg_reciprocal41.94
I(0) (reciprocal space) i0_reciprocal271400000.0000
Solution quality estimate total_estimate0.8565
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary51.7
Skewness Skewness skewness0.442
Kurtosis Kurtosis kurtosis-0.119
Angular range angular_range— – 0.1900 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha12770000.0000
Real-space data points n_real_points39
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.780; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.939; Smooth: 0.853

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 20 domains

SCOP 2.08 (8 domains)

Domain ID domain_idd3kfda_
Class classg — Small proteins
Fold Fold foldg.17 — Cystine-knot cytokines
Superfamily Superfamily superfamilyg.17.1 — Cystine-knot cytokines
Family Family familyg.17.1.2 — Transforming growth factor (TGF)-beta
Domain ID domain_idd3kfdb_
Class classg — Small proteins
Fold Fold foldg.17 — Cystine-knot cytokines
Superfamily Superfamily superfamilyg.17.1 — Cystine-knot cytokines
Family Family familyg.17.1.2 — Transforming growth factor (TGF)-beta
Domain ID domain_idd3kfdc_
Class classg — Small proteins
Fold Fold foldg.17 — Cystine-knot cytokines
Superfamily Superfamily superfamilyg.17.1 — Cystine-knot cytokines
Family Family familyg.17.1.2 — Transforming growth factor (TGF)-beta
Domain ID domain_idd3kfdd_
Class classg — Small proteins
Fold Fold foldg.17 — Cystine-knot cytokines
Superfamily Superfamily superfamilyg.17.1 — Cystine-knot cytokines
Family Family familyg.17.1.2 — Transforming growth factor (TGF)-beta
Domain ID domain_idd3kfde_
Class classg — Small proteins
Fold Fold foldg.7 — Snake toxin-like
Superfamily Superfamily superfamilyg.7.1 — Snake toxin-like
Family Family familyg.7.1.3 — Extracellular domain of cell surface receptors
Domain ID domain_idd3kfdf_
Class classg — Small proteins
Fold Fold foldg.7 — Snake toxin-like
Superfamily Superfamily superfamilyg.7.1 — Snake toxin-like
Family Family familyg.7.1.3 — Extracellular domain of cell surface receptors
Domain ID domain_idd3kfdg_
Class classg — Small proteins
Fold Fold foldg.7 — Snake toxin-like
Superfamily Superfamily superfamilyg.7.1 — Snake toxin-like
Family Family familyg.7.1.3 — Extracellular domain of cell surface receptors
Domain ID domain_idd3kfdh_
Class classg — Small proteins
Fold Fold foldg.7 — Snake toxin-like
Superfamily Superfamily superfamilyg.7.1 — Snake toxin-like
Family Family familyg.7.1.3 — Extracellular domain of cell surface receptors

CATH v4.4 (12 domains)

Domain ID domain_id3kfdA00
Class class2 — Mainly Beta
Architecture architecture10 — Ribbon
Topology topology90 — Cystine Knot Cytokines, subunit B
Homologous superfamily homologous superfamily10 — Cystine-knot cytokines
Domain ID domain_id3kfdB00
Class class2 — Mainly Beta
Architecture architecture10 — Ribbon
Topology topology90 — Cystine Knot Cytokines, subunit B
Homologous superfamily homologous superfamily10 — Cystine-knot cytokines
Domain ID domain_id3kfdC00
Class class2 — Mainly Beta
Architecture architecture10 — Ribbon
Topology topology90 — Cystine Knot Cytokines, subunit B
Homologous superfamily homologous superfamily10 — Cystine-knot cytokines
Domain ID domain_id3kfdD00
Class class2 — Mainly Beta
Architecture architecture10 — Ribbon
Topology topology90 — Cystine Knot Cytokines, subunit B
Homologous superfamily homologous superfamily10 — Cystine-knot cytokines
Domain ID domain_id3kfdE00
Class class2 — Mainly Beta
Architecture architecture10 — Ribbon
Topology topology60 — CD59
Homologous superfamily homologous superfamily10 — CD59
Domain ID domain_id3kfdF00
Class class2 — Mainly Beta
Architecture architecture10 — Ribbon
Topology topology60 — CD59
Homologous superfamily homologous superfamily10 — CD59
Domain ID domain_id3kfdG00
Class class2 — Mainly Beta
Architecture architecture10 — Ribbon
Topology topology60 — CD59
Homologous superfamily homologous superfamily10 — CD59
Domain ID domain_id3kfdH00
Class class2 — Mainly Beta
Architecture architecture10 — Ribbon
Topology topology60 — CD59
Homologous superfamily homologous superfamily10 — CD59
Domain ID domain_id3kfdI00
Class class2 — Mainly Beta
Architecture architecture10 — Ribbon
Topology topology60 — CD59
Homologous superfamily homologous superfamily10 — CD59
Domain ID domain_id3kfdJ00
Class class2 — Mainly Beta
Architecture architecture10 — Ribbon
Topology topology60 — CD59
Homologous superfamily homologous superfamily10 — CD59
Domain ID domain_id3kfdK00
Class class2 — Mainly Beta
Architecture architecture10 — Ribbon
Topology topology60 — CD59
Homologous superfamily homologous superfamily10 — CD59
Domain ID domain_id3kfdL00
Class class2 — Mainly Beta
Architecture architecture10 — Ribbon
Topology topology60 — CD59
Homologous superfamily homologous superfamily10 — CD59

8. Citations (1)

9. Files and Curves (10)