5oaq

TEAD4 COMPLEXED WITH YAP PEPTIDE AND MYRISTATE (COVALENTLY BOUND)

Method: X-RAY DIFFRACTION Dmax: 64.4 Å Quality: REASONABLE

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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 217–434 Fragment:C-terminal domain, YAP binding domain Transcriptional coactivator YAP1 × 1 (P46937) GOL GLYCEROL × 1 MYR MYRISTIC ACID × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6;298 K;15% PEG 3350,2% tacsimate, 0.1M NaCitrate Resolution 1.95 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.

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 3–220; UniProt 217–434

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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain L; UniProt 60–100 Not recorded Transcriptional enhancer factor TEF-3 × 1 (Q15561) GOL GLYCEROL × 1 MYR MYRISTIC ACID × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6;298 K;15% PEG 3350,2% tacsimate, 0.1M NaCitrate Resolution 1.95 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.

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
PDB entities 2
Chains and sequence ranges Author chain L; PDBConstruct 1–41; UniProt 60–100

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 5oaq

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 5oaq
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2. Structure Basics 2. Structure Basics

Entry ID entry_id5oaq
Deposition date deposition_date2017-06-23
Structure title titleTEAD4 COMPLEXED WITH YAP PEPTIDE AND MYRISTATE (COVALENTLY BOUND)
Keywords keywordsOTHER, TRANSCRIPTION; TRANSCRIPTION
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier19.95
Radius of gyration Rg (electron density) rg_electron18.36
Forward intensity I(0) i013956600.00
Molecular weight molecular_weight28597.0 kDa
Excluded volume excluded_volume36047 ų
Envelope volume envelope_volume41970 ų
Hydration-shell volume shell_volume19120 ų
Envelope diameter envelope_diameter68.6
Shell Rg shell_rg24.77
Envelope Rg envelope_rg18.75
Shape Rg shape_rg18.36
Total Rg total_rg19.34
Total atoms total_atoms2016
Residues n_residues244
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 dmax64.4
Rg (real space) rg_real19.83
Rg uncertainty (real space) rg_real_error0.39
I(0) (real space) i0_real1.3960e+07
I(0) uncertainty (real space) i0_real_error1.8090e+05
Rg (reciprocal space) rg_reciprocal19.85
I(0) (reciprocal space) i0_reciprocal13960000.0000
Solution quality estimate total_estimate0.6293
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary25.4
Skewness Skewness skewness0.168
Kurtosis Kurtosis kurtosis-0.372
Angular range angular_range— – 0.4000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha2632000.0000
Real-space data points n_real_points72
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.851; Stabil: 0.999; Sysdev: 0.210; Positv: 1.000; Valcen: 1.000; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

7. Fold Classification (SCOP + CATH) 2 domains

CATH v4.4 (2 domains)

Domain ID domain_id5oaqA00
Class class2 — Mainly Beta
Architecture architecture70 — Distorted Sandwich
Topology topology50 — Coagulation Factor XIII; Chain A, domain 1
Homologous superfamily homologous superfamily80
Domain ID domain_id5oaqL01
Class class6 — Special
Architecture architecture20 — Other non-globular
Topology topology430 — Virus Scaffolding Protein; Chain A
Homologous superfamily homologous superfamily10

8. Citations (1)

9. Files and Curves (10)