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UniProt Q15561

Transcriptional enhancer factor TEF-3 (Q15561)

Transcriptional enhancer factor TEF-3 (UniProt Q15561): 37 experimental structures and 1 predicted model on GenesisL1, 7 ligands bound, 67 pockets. Binding sites, druggability and experiment against prediction (TM-score) in GL1X.

UniProt
Q15561
Protein
Transcriptional enhancer factor TEF-3
Experimental structures
37
Predicted models
1
Ligands
7
Pockets
67 · 18 records with a druggable one

Structures

38 records of Q15561 in the MolNFT archive: 37 experimental, 1 predicted.

EntryTitleMethodChainsLigandsPockets
5GZBCrystal Structure of Transcription Factor TEAD4 in Complex with M-CAT DNAx-ray diffractionA——
5GZBCrystal structure of transcription factor TEAD4 in complex with M-cat DNAx-ray diffractionA——
5NO6TEAD4-HOXB13 complex bound to DNAx-ray diffractionI, N—4 (best 0.59)
5NO6TEAD4-HOXB13 complex bound to DNAx-ray diffractionI, N——
5OAQTEAD4 complexed with yap peptide and myristate (covalently bound)x-ray diffractionAMYR—
5OAQTEAD4 complexed with yap peptide and myristate (covalently bound)x-ray diffractionAMYR—
6GE3X-ray structure of TEAD4 (wildtype) complexed with YAP (wildtype): The role of residual flexibility…x-ray diffractionAMYR3 (best 0.81)
6GE3X-ray structure of TEAD4 (wildtype) complexed with yap (wildtype): the role of residual flexibility…x-ray diffractionAMYR—
6GE4TEAD4 (216-434);E263A complexed with yap peptide (60-100) and myristoate (covalently bound) at…x-ray diffractionAMYR2 (best 0.83)
6GE4TEAD4 (216-434);E263A complexed with yap peptide (60-100) and myristoate (covalently bound) at…x-ray diffractionAMYR—
6GE5TEAD4 (216-434);Y429F complexed with yap peptide (60-100) and myristoate (covalently bound) at…x-ray diffractionAMYR3 (best 0.83)
6GE5TEAD4 (216-434);Y429F complexed with yap peptide (60-100) and myristoate (covalently bound) at…x-ray diffractionAMYR—
6GE6X-ray structure of TEAD4(E263A+Y429F mutant) complexed with YAP(wildtype): The role of residual…x-ray diffractionAMYR, PO45 (best 0.83)
6GE6X-ray structure of TEAD4(E263A+Y429F mutant) complexed with YAP(WILDTYPE): the role of residual…x-ray diffractionAMYR, PO4—
6GECTEAD4 (216-434) complexed with yap peptide (60-100);S94A and myristoate (covalently bound) at 1.70A…x-ray diffractionAMYR3 (best 0.81)
6GECTEAD4 (216-434) complexed with yap peptide (60-100);S94A and myristoate (covalently bound) at 1.70A…x-ray diffractionAMYR—
6GEETEAD4 (216-434);E263A complexed with yap peptide (60-100); S94A and myristoate (covalently bound)…x-ray diffractionAMYR2 (best 0.81)
6GEETEAD4 (216-434);E263A complexed with yap peptide (60-100); S94A and myristoate (covalently bound)…x-ray diffractionAMYR—
6GEGTEAD4 (216-434);Y429F complexed with yap peptide (60-100); S94A and myristoate (covalently bound)…x-ray diffractionAMYR3 (best 0.82)
6GEGTEAD4 (216-434);Y429F complexed with yap peptide (60-100); S94A and myristoate (covalently bound)…x-ray diffractionAMYR—
6GEITEAD4 (216-434);E263A+Y429F complexed with yap peptide (60- 100);S94A and myristoate (covalently…x-ray diffractionAMYR, PO43 (best 0.83)
6GEITEAD4 (216-434);E263A+Y429F complexed with yap peptide (60- 100);S94A and myristoate (covalently…x-ray diffractionAMYR, PO4—
6GEKTEAD4 (216-434);Y429F complexed with yap peptide (60-100) and myristoate (covalently bound) at…x-ray diffractionA, BMYR5 (best 0.83)
6GEKTEAD4 (216-434);Y429F complexed with yap peptide (60-100) and myristoate (covalently bound) at…x-ray diffractionA, BMYR—
6HIKX-ray structure of TEAD4(Y429H) mutant) complexed with YAP (wildtype): Molecular and structural…x-ray diffractionAMYR, PO42 (best 0.83)
6HIKX-ray structure of TEAD4(Y429H) mutant) complexed with yap (wildtype): molecular and structural…x-ray diffractionAMYR, PO4—
6Q2XTEAD4 (216-434) complexed with yap peptide (60-100) and myristoate (covalently bound) at 2.1A…x-ray diffractionAMYR3 (best 0.82)
6Q2XTEAD4 (216-434) complexed with yap peptide (60-100) and myristoate (covalently bound) at 2.1A…x-ray diffractionAMYR—
6Q36TEAD4(216-434) complexed with optimized peptide 9 and myristoate (covalently bound) at 2.01A…x-ray diffractionA, BMYR, PO47 (best 0.83)
6Q36TEAD4(216-434) complexed with optimized peptide 9 and myristoate (covalently bound) at 2.01A…x-ray diffractionA, B2JH, MYR, PO4—
6SENTEAD4 bound to a FAM181A peptidex-ray diffractionA, BSO43 (best 0.74)
6SENTEAD4 bound to a FAM181A peptidex-ray diffractionA, BNH2, SO4—
6SEOTEAD4 bound to a FAM181B peptidex-ray diffractionA——
6SEOTEAD4 bound to a FAM181B peptidex-ray diffractionA——
8A8RCrystal structure of TEAD4 in complex with YAP peptidex-ray diffractionA, BMYR8 (best 0.84)
8C17Crystal structure of TEAD4 in complex with peptide 1x-ray diffractionAMYR2 (best 0.83)
8CAACrystal structure of TEAD4 in complex with YTP-13x-ray diffractionA, BU3F, U3O, PO45 (best 0.84)
Q15561AlphaFold monomer V2.0 prediction for transcriptional enhancer factor tef-3 (Q15561)predictedA—4 (best 0.81)

Ligands

  • MYR · Myristic acid · in 28 records
  • PO4 · Phosphate ion · in 9 records
  • SO4 · Sulfate ion · in 2 records
  • 2JH · 3-cyclobutyl-L-alanine · in 1 record
  • NH2 · Amino group · in 1 record
  • 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 · in 1 record
  • U3O · (2~{R})-2-[2-chloranyl-5-[2-chloranyl-4-(trifluoromethyl)phenoxy]phenyl]sulfanylpropanoic acid · in 1 record

Experiment against prediction

Elsewhere

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