5tx4

Derivative of mouse TGF-beta2, with a deletion of residues 52-71 and K25R, R26K, L51R, A74K, C77S, L89V, I92V, K94R T95K, I98V single amino acid substitutions, bound to human TGF-beta type II receptor ectodomain residues 15-130

Method: X-RAY DIFFRACTION Dmax: 86.3 Å Quality: REASONABLE

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 monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 38–153 Fragment:UNP residues 38-153 No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.5;298 K;0.1 M Hepes, pH 7.5, 60 % v/v (+/-)-2-Methyl-2,4-pentanediol Resolution 1.88 Å R-free 0.222

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 1–116; UniProt 38–153

Transforming growth factor beta-2

Homo sapiens

UniProt P61812

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
2 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain B; UniProt 303–414 Fragment:UNP residues 303-414 Mutation:deletion of residues 52-71 and K25R, R26K, L51R, A74K, C77S, L89V, I92V, K94R T95K, I98V No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.5;298 K;0.1 M Hepes, pH 7.5, 60 % v/v (+/-)-2-Methyl-2,4-pentanediol Resolution 1.88 Å R-free 0.222

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.

9 other PDB entries and 11 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name TGFB2_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–92; UniProt 303–414

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 5tx4

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 5tx4
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id5tx4
Deposition date deposition_date2016-11-15
Structure title titleDerivative of mouse TGF-beta2, with a deletion of residues 52-71 and K25R, R26K, L51R, A74K, C77S, L89V, I92V, K94R T95K, I98V single amino acid substitutions, bound to human TGF-beta type II receptor ectodomain residues 15-130
Keywords keywordsTGF-beta, TGF-beta type II receptor, TRANSFERASE-CYTOKINE complex; TRANSFERASE/CYTOKINE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier23.82
Radius of gyration Rg (electron density) rg_electron23.59
Forward intensity I(0) i09704170.00
Molecular weight molecular_weight22660.0 kDa
Excluded volume excluded_volume28080 ų
Envelope volume envelope_volume35644 ų
Hydration-shell volume shell_volume14493 ų
Envelope diameter envelope_diameter86.4
Shell Rg shell_rg27.06
Envelope Rg envelope_rg24.24
Shape Rg shape_rg23.58
Total Rg total_rg24.09
Total atoms total_atoms3070
Residues n_residues199
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 dmax86.3
Rg (real space) rg_real24.28
Rg uncertainty (real space) rg_real_error0.89
I(0) (real space) i0_real9.7040e+06
I(0) uncertainty (real space) i0_real_error1.5440e+05
Rg (reciprocal space) rg_reciprocal24.17
I(0) (reciprocal space) i0_reciprocal9704000.0000
Solution quality estimate total_estimate0.7091
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary18.9
Skewness Skewness skewness0.591
Kurtosis Kurtosis kurtosis-0.490
Angular range angular_range— – 0.3350 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha1013000.0000
Real-space data points n_real_points65
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.375; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.125; Smooth: 0.963

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd5tx4a_
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_idd5tx4b_
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

CATH v4.4 (2 domains)

Domain ID domain_id5tx4A00
Class class2 — Mainly Beta
Architecture architecture10 — Ribbon
Topology topology60 — CD59
Homologous superfamily homologous superfamily10 — CD59
Domain ID domain_id5tx4B00
Class class2 — Mainly Beta
Architecture architecture10 — Ribbon
Topology topology90 — Cystine Knot Cytokines, subunit B
Homologous superfamily homologous superfamily10 — Cystine-knot cytokines

8. Citations (1)

9. Files and Curves (10)