8a8r

Crystal structure of TEAD4 in complex with YAP peptide

Method: X-RAY DIFFRACTION Dmax: 86.0 Å Quality: GOOD

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

Transcriptional enhancer factor TEF-3

Homo sapiens

UniProt Q15561

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 heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 216–434 Chain B; UniProt 216–434 Fragment:C-terminal domain, YAP binding domain Isoform 7 of Transcriptional coactivator YAP1 × 2 (P46937) MYR MYRISTIC ACID × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;293 K;50 mM sodium acetate trihydrate pH 4.6 50 mM magnesium acetate tetrahydrate 25% PEG400 Resolution 1.70 Å R-free 0.243

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.

22 other PDB entries and 26 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name TEAD4_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–219; UniProt 216–434 Author chain B; PDBConstruct 1–219; UniProt 216–434

Isoform 7 of Transcriptional coactivator YAP1

OrganismNot specified

UniProt P46937

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 heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain L; UniProt 50–100 Chain M; UniProt 50–100 Non-standard monomer:Yes (specific site not provided by mmCIF) Transcriptional enhancer factor TEF-3 × 2 (Q15561) MYR MYRISTIC ACID × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;293 K;50 mM sodium acetate trihydrate pH 4.6 50 mM magnesium acetate tetrahydrate 25% PEG400 Resolution 1.70 Å R-free 0.243

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.

31 other PDB entries and 38 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name YAP1_HUMAN
Isoform P46937-7
PDB entities 2
Chains and sequence ranges Author chain L; PDBConstruct 2–52; UniProt 50–100 Author chain M; PDBConstruct 2–52; UniProt 50–100

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 8a8r

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8a8r
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8a8r
Deposition date deposition_date2022-06-23
Structure title titleCrystal structure of TEAD4 in complex with YAP peptide
Keywords keywordsComplex, TRANSCRIPTION; TRANSCRIPTION
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier26.89
Radius of gyration Rg (electron density) rg_electron26.27
Forward intensity I(0) i049584800.00
Molecular weight molecular_weight56252.0 kDa
Excluded volume excluded_volume71048 ų
Envelope volume envelope_volume86584 ų
Hydration-shell volume shell_volume27954 ų
Envelope diameter envelope_diameter90.0
Shell Rg shell_rg33.13
Envelope Rg envelope_rg26.24
Shape Rg shape_rg26.23
Total Rg total_rg27.16
Total atoms total_atoms3969
Residues n_residues484
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 dmax86.0
Rg (real space) rg_real26.95
Rg uncertainty (real space) rg_real_error0.47
I(0) (real space) i0_real4.9580e+07
I(0) uncertainty (real space) i0_real_error6.6890e+05
Rg (reciprocal space) rg_reciprocal26.93
I(0) (reciprocal space) i0_reciprocal49580000.0000
Solution quality estimate total_estimate0.8897
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary29.1
Skewness Skewness skewness0.407
Kurtosis Kurtosis kurtosis-0.435
Angular range angular_range— – 0.2950 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha11710000.0000
Real-space data points n_real_points60
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.881; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.964; Smooth: 0.955

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 2 domains

CATH v4.4 (2 domains)

Domain ID domain_id8a8rA01
Class class2 — Mainly Beta
Architecture architecture70 — Distorted Sandwich
Topology topology50 — Coagulation Factor XIII; Chain A, domain 1
Homologous superfamily homologous superfamily80
Domain ID domain_id8a8rB01
Class class2 — Mainly Beta
Architecture architecture70 — Distorted Sandwich
Topology topology50 — Coagulation Factor XIII; Chain A, domain 1
Homologous superfamily homologous superfamily80

8. Citations (1)

9. Files and Curves (10)