8pom

TEAD2 in complex with an inhibitor

Method: X-RAY DIFFRACTION Dmax: 74.0 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 monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain B; UniProt 217–447 Not recorded ZUP 2-[[3-(2-phenylethoxy)phenyl]amino]pyridine-3-carboxylic acid × 1 GOL GLYCEROL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;298 K;2.8M sodium formate Resolution 1.95 Å R-free 0.248
2 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 217–447 Not recorded ZUP 2-[[3-(2-phenylethoxy)phenyl]amino]pyridine-3-carboxylic acid × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;298 K;2.8M sodium formate Resolution 1.95 Å R-free 0.248

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 78 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 8pom

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id8pom
Deposition date deposition_date2023-07-05
最后修订 last_revision2023-11-22
Structure title titleTEAD2 in complex with an inhibitor
Keywords keywordsInhibitor, TEAD, Complex, 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_guinier23.67
Radius of gyration Rg (electron density) rg_electron22.37
Forward intensity I(0) i037643600.00
Molecular weight molecular_weight47891.0 kDa
Excluded volume excluded_volume60191 ų
Envelope volume envelope_volume72161 ų
Hydration-shell volume shell_volume26441 ų
Envelope diameter envelope_diameter76.7
Shell Rg shell_rg29.57
Envelope Rg envelope_rg22.57
Shape Rg shape_rg22.39
Total Rg total_rg23.23
Total atoms total_atoms3427
Residues n_residues408
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 dmax74.0
Rg (real space) rg_real23.54
Rg uncertainty (real space) rg_real_error0.34
I(0) (real space) i0_real3.7640e+07
I(0) uncertainty (real space) i0_real_error4.6230e+05
Rg (reciprocal space) rg_reciprocal23.58
I(0) (reciprocal space) i0_reciprocal37640000.0000
Solution quality estimate total_estimate0.9037
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary28.9
Skewness Skewness skewness0.176
Kurtosis Kurtosis kurtosis-0.460
Angular range angular_range— – 0.3350 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha6744000.0000
Real-space data points n_real_points65
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.918; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.995; Smooth: 0.995

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)