8ygz

The Crystal Structure of TGF beta R2 kinase domain from Biortus.

Method: X-RAY DIFFRACTION Dmax: 67.1 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 237–549 Non-standard monomer:Yes (specific site not provided by mmCIF) EDO 1,2-ETHANEDIOL × 10 PEG DI(HYDROXYETHYL)ETHER × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;293 K;0.2M Li2SO4, 0.1M Tris-HCl pH8.5, 30% PEG4,000 Resolution 2.10 Å R-free 0.254

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 2–314; UniProt 237–549

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 8ygz

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8ygz
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id8ygz
Deposition date deposition_date2024-02-27
Structure title titleThe Crystal Structure of TGF beta R2 kinase domain from Biortus.
Keywords keywordsSerine/threonine-protein kinase, transferase, apoptosis, ATP-binding; TRANSFERASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier20.19
Radius of gyration Rg (electron density) rg_electron19.19
Forward intensity I(0) i019693800.00
Molecular weight molecular_weight33610.0 kDa
Excluded volume excluded_volume42074 ų
Envelope volume envelope_volume49103 ų
Hydration-shell volume shell_volume21104 ų
Envelope diameter envelope_diameter68.7
Shell Rg shell_rg25.89
Envelope Rg envelope_rg19.59
Shape Rg shape_rg19.19
Total Rg total_rg20.10
Total atoms total_atoms2357
Residues n_residues289
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 dmax67.1
Rg (real space) rg_real20.10
Rg uncertainty (real space) rg_real_error0.36
I(0) (real space) i0_real1.9690e+07
I(0) uncertainty (real space) i0_real_error2.5160e+05
Rg (reciprocal space) rg_reciprocal20.12
I(0) (reciprocal space) i0_reciprocal19690000.0000
Solution quality estimate total_estimate0.8778
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary25.9
Skewness Skewness skewness0.224
Kurtosis Kurtosis kurtosis-0.323
Angular range angular_range— – 0.3950 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha6544000.0000
Real-space data points n_real_points71
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.812; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.998; Smooth: 0.971

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)