4p7u

Extracellular domain of type II Transforming Growth Factor Beta receptor in complex with NDSB-201

Method: X-RAY DIFFRACTION Dmax: 45.4 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 monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 75–184 Fragment:extracellular domain, UNP residues 74-175 Mutation:Q26A K97T 1PS 3-PYRIDINIUM-1-YLPROPANE-1-SULFONATE × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5;298 K;100 mM sodium citrate, 30% PEG 2000 Resolution 1.50 Å R-free 0.206

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 3–112; UniProt 75–184

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 4p7u

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4p7u
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2. Structure Basics 2. Structure Basics

Entry ID entry_id4p7u
Deposition date deposition_date2014-03-27
Structure title titleExtracellular domain of type II Transforming Growth Factor Beta receptor in complex with NDSB-201
Keywords keywordsNDSB-201, type II Transforming Growth Factor Beta receptor, SIGNALING PROTEIN; SIGNALING PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier13.75
Radius of gyration Rg (electron density) rg_electron12.77
Forward intensity I(0) i03156310.00
Molecular weight molecular_weight11740.0 kDa
Excluded volume excluded_volume14365 ų
Envelope volume envelope_volume15968 ų
Hydration-shell volume shell_volume10664 ų
Envelope diameter envelope_diameter44.0
Shell Rg shell_rg18.53
Envelope Rg envelope_rg13.23
Shape Rg shape_rg12.78
Total Rg total_rg13.96
Total atoms total_atoms810
Residues n_residues102
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 dmax45.4
Rg (real space) rg_real13.69
Rg uncertainty (real space) rg_real_error0.24
I(0) (real space) i0_real3.1560e+06
I(0) uncertainty (real space) i0_real_error3.2650e+04
Rg (reciprocal space) rg_reciprocal13.69
I(0) (reciprocal space) i0_reciprocal3156000.0000
Solution quality estimate total_estimate0.8806
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary16.7
Skewness Skewness skewness0.247
Kurtosis Kurtosis kurtosis-0.280
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha839500.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.824; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.999; Smooth: 0.973

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 3 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd4p7ua1
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_idd4p7ua2
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags

CATH v4.4 (1 domains)

Domain ID domain_id4p7uA00
Class class2 — Mainly Beta
Architecture architecture10 — Ribbon
Topology topology60 — CD59
Homologous superfamily homologous superfamily10 — CD59

8. Citations (1)

9. Files and Curves (10)