8puy

TEAD2 with a covalent inhibitor

Method: X-RAY DIFFRACTION Dmax: 73.7 Å Quality: EXCELLENT

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

Transcriptional enhancer factor TEF-4

Homo sapiens

UniProt Q15562

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 homooligomer Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 217–447 Chain B; UniProt 217–447 Not recorded F3Y ~{N}-[3-[(3-pentoxyphenyl)amino]phenyl]propanamide × 1 MYR MYRISTIC ACID × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;298 K;2.8M sodium formate Resolution 2.20 Å R-free 0.252

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.

41 other PDB entries and 79 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name TEAD2_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 2–232; UniProt 217–447 Author chain B; PDBConstruct 2–232; UniProt 217–447

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 8puy

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8puy
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8puy
Deposition date deposition_date2023-07-17
Structure title titleTEAD2 with a covalent inhibitor
Keywords keywordsTEAD2, Inhibitor, Covalent, 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_guinier23.77
Radius of gyration Rg (electron density) rg_electron22.40
Forward intensity I(0) i036554200.00
Molecular weight molecular_weight47364.0 kDa
Excluded volume excluded_volume59656 ų
Envelope volume envelope_volume72138 ų
Hydration-shell volume shell_volume26464 ų
Envelope diameter envelope_diameter76.0
Shell Rg shell_rg29.59
Envelope Rg envelope_rg22.56
Shape Rg shape_rg22.42
Total Rg total_rg23.27
Total atoms total_atoms3345
Residues n_residues406
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 dmax73.7
Rg (real space) rg_real23.64
Rg uncertainty (real space) rg_real_error0.31
I(0) (real space) i0_real3.6550e+07
I(0) uncertainty (real space) i0_real_error4.4350e+05
Rg (reciprocal space) rg_reciprocal23.67
I(0) (reciprocal space) i0_reciprocal36550000.0000
Solution quality estimate total_estimate0.9054
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary29.9
Skewness Skewness skewness0.179
Kurtosis Kurtosis kurtosis-0.457
Angular range angular_range— – 0.3350 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha6885000.0000
Real-space data points n_real_points65
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.926; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.994; Smooth: 0.994

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)