SAXSdb — 9qkq

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

Transcriptional enhancer factor TEF-3

Homo sapiens

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	Not recorded	peptide 6 × 1 EDO 1,2-ETHANEDIOL × 9 MYR MYRISTIC ACID × 1	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, SITTING DROP；293 K；0.9-1.2 M sodium/potassium phosphate buffer at pH 5.6	Resolution 1.74 Å R-free 0.221
2	Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain B； UniProt 217–434	Not recorded	peptide 6 × 1 EDO 1,2-ETHANEDIOL × 1 MYR MYRISTIC ACID × 1 PO4 PHOSPHATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, SITTING DROP；293 K；0.9-1.2 M sodium/potassium phosphate buffer at pH 5.6	Resolution 1.74 Å R-free 0.221

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.

Other PDB	Difference from Current Entry 9QKQ	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
5GZB Crystal Structure of Transcription Factor TEAD4 in Complex with M-CAT DNA Deposited 2016-09-28	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein–DNA Monomer；Protein × 1 PDB declaration: trimeric	Chain A 36–139（104 aa） Fragment：UNP residues 36-139	Non-standard monomer：Yes (specific site not provided by mmCIF)	GOL GLYCEROL × 1 PO4 PHOSPHATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.5；291 K；0.6 M Na2HPO4, 0.6 M KH2PO4, 0.1 M HEPES	Resolution 2.70 Å R-free 0.256
5NO6 TEAD4-HOXB13 complex bound to DNA Deposited 2017-04-11	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein–DNA Heteromer；Protein × 2 PDB declaration: tetrameric	Chain N 40–112（73 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.24；298 K；PEG (4000), Ammonium sulphate, PME(550, MOPs	Resolution 2.88 Å R-free 0.317
5NO6 TEAD4-HOXB13 complex bound to DNA Deposited 2017-04-11	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein–DNA Heteromer；Protein × 2 PDB declaration: tetrameric	Chain I 40–112（73 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.24；298 K；PEG (4000), Ammonium sulphate, PME(550, MOPs	Resolution 2.88 Å R-free 0.317
5OAQ TEAD4 COMPLEXED WITH YAP PEPTIDE AND MYRISTATE (COVALENTLY BOUND) Deposited 2017-06-23	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 217–434（218 aa） Fragment：C-terminal domain, YAP binding domain	Not recorded	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
6GE3 X-ray structure of TEAD4 (wildtype) complexed with YAP (wildtype): The role of residual flexibility and water molecules in the adaptation of a bound intrinsically disordered protein to mutations at a binding interface Deposited 2018-04-25	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 216–434（219 aa） Fragment：C-terminal domain, YAP binding domain	Not recorded	MYR MYRISTIC ACID × 1 GOL GLYCEROL × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6；298 K；16% PEG 3350,2% tacsimate, 0.1M NaCit, pH 5.6	Resolution 1.85 Å R-free 0.242
6GE4 TEAD4 (216-434);E263A COMPLEXED WITH YAP PEPTIDE (60-100) AND MYRISTOATE (COVALENTLY BOUND) AT 1.97A (P41212 CRYSTAL FORM); MYRISTOYLATION WAS DONE BY ADDING MYR-COA Deposited 2018-04-25	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 216–434（219 aa） Fragment：C-terminal domain, YAP binding domain	Not recorded	MYR MYRISTIC ACID × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；298 K；20% PEG 3350, 0.2M MgNitrate	Resolution 1.97 Å R-free 0.241
6GE5 TEAD4 (216-434);Y429F COMPLEXED WITH YAP PEPTIDE (60-100) AND MYRISTOATE (COVALENTLY BOUND) AT 2.05A (P41212 CRYSTAL FORM); MYRISTOYLATION WAS DONE BY ADDING MYR-COA Deposited 2018-04-25	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 216–434（219 aa） Fragment：C-terminal domain, YAP binding domain	Not recorded	MYR MYRISTIC ACID × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 4；298 K；20% PEG 3350, 8% Tacsimate	Resolution 2.05 Å R-free 0.238
6GE6 X-ray structure of TEAD4(E263A+Y429F mutant) complexed with YAP(wildtype): The role of residual flexibility and water molecules in the adaptation of a bound intrinsically disordered protein to mutations at a binding interface Deposited 2018-04-25	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 173–391（219 aa） Fragment：C-terminal domain, YAP binding domain	Not recorded	MYR MYRISTIC ACID × 1 PO4 PHOSPHATE ION × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.5；298 K；2M ammonium sulfate, 0.1M Bis-TRIS	Resolution 1.80 Å R-free 0.238
6GEC TEAD4 (216-434) COMPLEXED WITH YAP PEPTIDE (60-100);S94A AND MYRISTOATE (COVALENTLY BOUND) AT 1.70A (P41212 CRYSTAL FORM); MYRISTOYLATION WAS DONE BY ADDING MYR-COA Deposited 2018-04-26	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 216–434（219 aa） Fragment：C-terminal domain, YAP binding domain	Not recorded	MYR MYRISTIC ACID × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；298 K；20% PEG 3350, 0.2M NaTartrate	Resolution 1.70 Å R-free 0.242
6GEE TEAD4 (216-434);E263A COMPLEXED WITH YAP PEPTIDE (60-100); S94A AND MYRISTOATE (COVALENTLY BOUND) AT 1.96A (P41212 CRYSTAL FORM); MYRISTOYLATION WAS DONE BY ADDING MYR-COA Deposited 2018-04-26	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 216–434（219 aa） Fragment：C-terminal domain, YAP binding domain	Mutation：E263A	MYR MYRISTIC ACID × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.5；298 K；17% PEG 10000, 0.1M ammonium acetate, 0.1M Bis-TRIS	Resolution 1.96 Å R-free 0.245
6GEG TEAD4 (216-434);Y429F COMPLEXED WITH YAP PEPTIDE (60-100); S94A AND MYRISTOATE (COVALENTLY BOUND) AT 2.23A (P41212 CRYSTAL FORM); MYRISTOYLATION WAS DONE BY ADDING MYR-COA Deposited 2018-04-26	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 216–434（219 aa） Fragment：C-terminal domain, YAP binding domain	Mutation：Y429F	MYR MYRISTIC ACID × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；298 K；20% PEG 3350, 0.2M Na tartrate	Resolution 2.23 Å R-free 0.236
6GEI TEAD4 (216-434);E263A+Y429F COMPLEXED WITH YAP PEPTIDE (60- 100);S94A AND MYRISTOATE (COVALENTLY BOUND TO LYS344, NOT CYS367!) AT 1.65A (P41212 CRYSTAL FORM); MYRISTOYLATION WAS DONE BY ADDING MYR-COA Deposited 2018-04-26	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 216–434（219 aa） Fragment：C-terminal domain, YAP binding domain	Mutation：E263A+Y429F	MYR MYRISTIC ACID × 1 PO4 PHOSPHATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；298 K；20% PEG 3350, 0.2M Na acetate	Resolution 1.65 Å R-free 0.248
6GEK TEAD4 (216-434);Y429F COMPLEXED WITH YAP PEPTIDE (60-100) AND MYRISTOATE (COVALENTLY BOUND) AT 2.28A (P212121 CRYSTAL FORM); MYRISTOYLATION WAS DONE BY ADDING MYR-COA Deposited 2018-04-26	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 216–434（219 aa） Fragment：C-terminal domain, YAP binding domain	Mutation：Y429F	MYR MYRISTIC ACID × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.5；298 K；25% PEG 3350, 0.2M MgCl2, 0.1M Bis-TRIS	Resolution 2.28 Å R-free 0.246
6GEK TEAD4 (216-434);Y429F COMPLEXED WITH YAP PEPTIDE (60-100) AND MYRISTOATE (COVALENTLY BOUND) AT 2.28A (P212121 CRYSTAL FORM); MYRISTOYLATION WAS DONE BY ADDING MYR-COA Deposited 2018-04-26	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 216–434（219 aa） Fragment：C-terminal domain, YAP binding domain	Mutation：Y429F	MYR MYRISTIC ACID × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.5；298 K；25% PEG 3350, 0.2M MgCl2, 0.1M Bis-TRIS	Resolution 2.28 Å R-free 0.246
6HIK X-ray structure of TEAD4(Y429H) mutant) complexed with YAP (wildtype): Molecular and structural characterization of a TEAD mutation at the origin of Sveinsson's chorioretinal atrophy Deposited 2018-08-30	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 173–391（219 aa） Fragment：C-terminal domain, YAP binding domain	Not recorded	MYR MYRISTIC ACID × 1 PO4 PHOSPHATE ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.6；298 K；1.4M Na/K PO4	Resolution 1.65 Å R-free 0.237
6Q2X TEAD4 (216-434) COMPLEXED WITH YAP PEPTIDE (60-100) AND MYRISTOATE (COVALENTLY BOUND) AT 2.1A (P41212 CRYSTAL FORM) Deposited 2018-12-03	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 217–434（218 aa） Fragment：C-terminal domain, YAP binding domain	Not recorded	GOL GLYCEROL × 1 MYR MYRISTIC ACID × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.6；298 K；16% PEG 3350,2% tacsimate, 0.1M NaCit	Resolution 2.10 Å R-free 0.253
6Q36 TEAD4(216-434) complexed with optimized peptide 9 and myristoate (covalently bound) at 2.01A resolution: Structure-based design of potent linear peptide inhibitors of the YAP-TEAD protein-protein interaction derived from the YAP omega-loop sequence Deposited 2018-12-03	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain A 217–434（218 aa） Fragment：C-terminal domain, YAP binding domain Chain B 217–434（218 aa） Fragment：C-terminal domain, YAP binding domain	Not recorded	MYR MYRISTIC ACID × 2 PO4 PHOSPHATE ION × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.6；298 K；0.9 M NaK Phosphate	Resolution 2.01 Å R-free 0.244
6SEN TEAD4 bound to a FAM181A peptide Deposited 2019-07-30	Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 217–434（218 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF)	SO4 SULFATE ION × 3	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 4.59；293 K；200 mM Ammonium sulfate 100 mM Sodium acetate trihydrate pH 4.59 35% Pentaerythritol ethoxylate (15/4 EO/OH)	Resolution 1.65 Å R-free 0.219
6SEN TEAD4 bound to a FAM181A peptide Deposited 2019-07-30	Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 217–434（218 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF)	SO4 SULFATE ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 4.59；293 K；200 mM Ammonium sulfate 100 mM Sodium acetate trihydrate pH 4.59 35% Pentaerythritol ethoxylate (15/4 EO/OH)	Resolution 1.65 Å R-free 0.219
6SEO TEAD4 bound to a FAM181B peptide Deposited 2019-07-30	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 174–391（218 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF)	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.5；293 K；50 mM ammonium sulfate 50 mM Bis-TRIS pH 6.5 30% Pentaerythritol ethoxylate (15/4 EO/OH)	Resolution 2.55 Å R-free 0.232
8A8R Crystal structure of TEAD4 in complex with YAP peptide Deposited 2022-06-23	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain A 216–434（219 aa） Fragment：C-terminal domain, YAP binding domain Chain B 216–434（219 aa） Fragment：C-terminal domain, YAP binding domain	Not recorded	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
8C17 Crystal structure of TEAD4 in complex with peptide 1 Deposited 2022-12-20	Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain A 217–434（218 aa）	Not recorded	GOL GLYCEROL × 4 MYR MYRISTIC ACID × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；2.4 M sodium malonate	Resolution 2.25 Å R-free 0.238
8CAA Crystal structure of TEAD4 in complex with YTP-13 Deposited 2023-01-24	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 217–434（218 aa） Fragment：C-terminal domain, YAP binding domain Chain B 217–434（218 aa） Fragment：C-terminal domain, YAP binding domain	Not recorded	U3F 4-[bis(fluoranyl)methoxy]-2-[(2~{S})-5-chloranyl-6-fluoranyl-2-[[(4-oxidanylcyclohexyl)amino]methyl]-2-phenyl-3~{H}-1-benzofuran-4-yl]-3-fluoranyl-benzamide × 2 U3O (2~{R})-2-[2-chloranyl-5-[2-chloranyl-4-(trifluoromethyl)phenoxy]phenyl]sulfanylpropanoic acid × 2 PO4 PHOSPHATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；22% PEG 3350 (w/v) , 0.25 M ammonium citrate dibasic	Resolution 2.00 Å R-free 0.237
9SYI Crystal structure of TEAD4 in complex with compound 9 Deposited 2025-10-13	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 217–434（218 aa） Chain B 217–434（218 aa）	Not recorded	U3O (2~{R})-2-[2-chloranyl-5-[2-chloranyl-4-(trifluoromethyl)phenoxy]phenyl]sulfanylpropanoic acid × 2 A1ICN 2-[(2~{S})-5-chloranyl-2-phenyl-2-[(2~{S})-pyrrolidin-2-yl]-3~{H}-1-benzofuran-4-yl]-3-fluoranyl-4-methoxy-benzamide × 2 PO4 PHOSPHATE ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；sodium/potassium phosphate	Resolution 2.10 Å R-free 0.245
9SYN Crystal structure of TEAD4 in complex with Vgll1-peptide and IAG933 Deposited 2025-10-13	Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 217–434（218 aa）	Not recorded	MYR MYRISTIC ACID × 1 WCF 4-[(2~{S})-5-chloranyl-6-fluoranyl-2-phenyl-2-[(2~{S})-pyrrolidin-2-yl]-3~{H}-1-benzofuran-4-yl]-5-fluoranyl-6-(2-hydroxyethyloxy)-~{N}-methyl-pyridine-3-carboxamide × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；Ammonium sulfate, HEPES, PEG3350	Resolution 1.30 Å R-free 0.233

22 other PDB entries and 25 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 5–222； UniProt 217–434 Author chain B； PDBConstruct 5–222； UniProt 217–434

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.

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2. Structure Basics 2. Structure Basics

Entry ID entry_id	9qkq
Deposition date deposition_date	2025-03-20
最后修订 last_revision	2026-04-08
Structure title title	Crystal structure of hTEAD4 YAP binding domain (hTEAD4-YBD) in complex with peptide 6
Keywords keywords	human TEAD4, YAP binding domain, TRANSCRIPTION; TRANSCRIPTION
Experimental Method method	X-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier	26.14 Å
Radius of gyration Rg (electron density) rg_electron	25.61 Å
Forward intensity I(0) i0	44137200.00
Molecular weight molecular_weight	53102.0 kDa
Excluded volume excluded_volume	66994 Å³
Envelope volume envelope_volume	80769 Å³
Hydration-shell volume shell_volume	26853 Å³
Envelope diameter envelope_diameter	88.7 Å
Shell Rg shell_rg	32.39 Å
Envelope Rg envelope_rg	25.57 Å
Shape Rg shape_rg	25.59 Å
Total Rg total_rg	26.45 Å
Total atoms total_atoms	3748
Residues n_residues	444
Spherical-harmonic order n_harmonics	20
q range q_range	— – 0.5000 Å⁻¹
Data points n_points	101
Shell type shell_type	directional
Solvent electron density solvent_density	0.3340 e/Å³
Shell contrast contrast_shell	0.0300 e/Å³
CRYSOL version crysol_version	4.1.3

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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax	84.3 Å
Rg (real space) rg_real	26.21 Å
Rg uncertainty (real space) rg_real_error	0.52 Å
I(0) (real space) i0_real	4.4140e+07
I(0) uncertainty (real space) i0_real_error	5.9710e+05
Rg (reciprocal space) rg_reciprocal	26.19 Å
I(0) (reciprocal space) i0_reciprocal	44140000.0000
Solution quality estimate total_estimate	0.8888
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	27.6 Å
Skewness Skewness skewness	0.431
Kurtosis Kurtosis kurtosis	-0.353
Angular range angular_range	— – 0.3050 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	11180000.0000
Real-space data points n_real_points	62
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.877; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.976; Smooth: 0.944

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (6)

Entity 1 Entity 1 polymer

Description description	Transcriptional enhancer factor TEF-3
Molecular weight formula_weight	25857.1 kDa
Source method src_method	man
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B
Atom count atom_count	4388

GSHMRSVASSKLWMLEFSAFLEQQQDPDTYNKHLFVHIGQSSPSYSDPYLEAVDIRQIYDKFPEKKGGLKDLFERGPSNAFFLVKFWADLNTNIEDEGSSFYGVSSQYESPENMIITCSTKVCSFGKQVVEKVETEYARYENGHYSYRIHRSPLCEYMINFIHKLKHLPEKYMMNSVLENFTILQVVTNRDTQETLLCIAYVFEVSASEHGAQHHIYRLVKE

来源 Source

来源生物 organism	Homo sapiens
通用名 common_name	human
NCBI Class编号 ncbi_taxonomy_id	9606
宿主生物 host_organism	Escherichia coli

Entity 2 Entity 2 polymer

Description description	peptide 6
Molecular weight formula_weight	1996.8 kDa
Source method src_method	syn
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	C,D

XPWRLRKLPDSFAKPPX

Entity 3 Entity 3 non-polymer

Description description	1,2-ETHANEDIOL
Molecular weight formula_weight	62.1 kDa
Source method src_method	nat
Copy count entity_count	10

Entity 4 Entity 4 non-polymer

Description description	MYRISTIC ACID
Molecular weight formula_weight	228.4 kDa
Source method src_method	nat
Copy count entity_count	2

Entity 5 Entity 5 non-polymer

Description description	PHOSPHATE ION
Molecular weight formula_weight	95.0 kDa
Source method src_method	nat
Copy count entity_count	1

Entity 6 Entity 6 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	403

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8. Citations (1)

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Unit-cell length a length_a	171.538 Å
Unit-cell length b length_b	40.243 Å
Unit-cell length c length_c	97.892 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	92.77 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	8

Space group space_group	C 1 2 1
Space-group number int_tables_number	5
Crystal system crystal_system	—

Resolution resolution	1.740 Å
Low-resolution limit resolution_low	97.780 Å
R factor r_factor	0.1850
R_work r_work	0.1832
R_free r_free	0.2210

fit	/app/data/saxs_computation/qk/9qkq/9qkq.fit
pddf	/app/data/pr_computation/qk/9qkq/9qkq.pr.out
profile	/app/data/saxs_computation/qk/9qkq/9qkq.dat

Crystal structure of hTEAD4 YAP binding domain (hTEAD4-YBD) in complex with peptide 6

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

Transcriptional enhancer factor TEF-3

State in the Current Structure

Other States of the Same Protein in the Database

SAXS scattering curve SAXS Profile

P(r) Distance Distribution P(r) Distribution

2. Structure Basics 2. Structure Basics

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

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

5. Crystallography and Experiment 5. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

Diffraction experiment Diffraction

6. Entities and Polymers Entities & Polymers (6)

Entity 1 Entity 1 polymer

Polymer Polymer

来源 Source

Entity 2 Entity 2 polymer

Polymer Polymer

Entity 3 Entity 3 non-polymer

Entity 4 Entity 4 non-polymer

Entity 5 Entity 5 non-polymer

Entity 6 Entity 6 water

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)