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UniProt P46937

Transcriptional coactivator YAP1 (P46937)

Transcriptional coactivator YAP1 (UniProt P46937): 47 experimental structures on GenesisL1, 2 ligands bound, 11 pockets. Binding sites, pockets, druggability and 3D structures in GL1X.

UniProt
P46937
Protein
Transcriptional coactivator YAP1
Experimental structures
47
Predicted models
0
Ligands
2
Pockets
11 · 2 records with a druggable one

Structures

47 records of P46937 in the MolNFT archive: 47 experimental, 0 predicted.

EntryTitleMethodChainsLigandsPockets
1JMQYAP65 (L30K mutant) WW domain in Complex with GTPPPPYTVG peptidesolution nmrA——
1JMQYAP65 (L30K mutant) ww domain in complex with gtppppytvg peptidesolution nmrA——
1K5RYAP65 WW domain S24-Amino-Ethylsulfanyl-Acetic Acid mutantsolution nmrA——
1K5RYAP65 ww domain S24-amino-ethylsulfanyl-acetic acid mutantsolution nmrA——
1K9QYAP65 WW domain complexed to N-(n-octyl)-GPPPY-NH2solution nmrA——
1K9QYAP65 ww domain complexed to N-(N-octyl)-gpppy-NH2solution nmrA——
1K9RYAP65 WW domain complexed to Acetyl-PLPPYsolution nmrA——
1K9RYAP65 ww domain complexed to acetyl-plppysolution nmrA——
2LAWStructure of the second WW domain from human YAP in complex with a human Smad1 derived peptidesolution nmrA——
2LAWStructure of the second ww domain from human yap in complex with a human SMAD1 derived peptidesolution nmrA——
2LAXStructure of first WW domain of human YAP in complex with a human Smad1 doubly-phosphorilated…solution nmrA——
2LAXStructure of first ww domain of human yap in complex with a human SMAD1 doubly-phosphorilated…solution nmrA——
2LAYStructure of the first WW domain of human YAP in complex with a phosphorylated human Smad1 derived…solution nmrA——
2LAYStructure of the first ww domain of human yap in complex with a phosphorylated human SMAD1 derived…solution nmrA——
2LTVYAP WW2 in complex with a Smad7 derived peptidesolution nmrA——
2LTVYap WW2 in complex with a SMAD7 derived peptidesolution nmrA——
2LTWYAP WW1 in complex with a Smad7 derived peptidesolution nmrA——
2LTWYap WW1 in complex with a SMAD7 derived peptidesolution nmrA——
3KYSCrystal structure of human YAP and TEAD complexx-ray diffractionB, D——
3KYSCrystal structure of human yap and tead complexx-ray diffractionB, D——
4RE1Crystal structure of human TEAD1 and disulfide-engineered YAPx-ray diffractionC, D——
4RE1Crystal structure of human TEAD1 and disulfide-engineered yapx-ray diffractionC, D——
4REXCrystal structure of the first WW domain of human YAP2 isoformx-ray diffractionA——
4REXCrystal structure of the first ww domain of human YAP2 isoformx-ray diffractionA——
5OAQTEAD4 complexed with yap peptide and myristate (covalently bound)x-ray diffractionL——
5OAQTEAD4 complexed with yap peptide and myristate (covalently bound)x-ray diffractionL——
6G6X14-3-3SIGMA in complex with a P129BETA3P mutated yap PS127 phosphopeptidex-ray diffractionPEOE—
6G8P14-3-3sigma in complex with a P129beta3P and L132beta3L mutated YAP pS127 phosphopeptidex-ray diffractionP—1 (best 0.52)
6G8P14-3-3SIGMA in complex with a P129BETA3P and L132BETA3L mutated yap PS127 phosphopeptidex-ray diffractionPEOE—
6G8Q14-3-3SIGMA in complex with a A130BETA3A and Q133BETA3Q mutated yap PS127 phosphopeptidex-ray diffractionP——
6GE3X-ray structure of TEAD4 (wildtype) complexed with YAP (wildtype): The role of residual flexibility…x-ray diffractionL—1 (best 0.31)
6GE3X-ray structure of TEAD4 (wildtype) complexed with yap (wildtype): the role of residual flexibility…x-ray diffractionL——
6GE4TEAD4 (216-434);E263A complexed with yap peptide (60-100) and myristoate (covalently bound) at…x-ray diffractionL——
6GE5TEAD4 (216-434);Y429F complexed with yap peptide (60-100) and myristoate (covalently bound) at…x-ray diffractionL——
6GE6X-ray structure of TEAD4(E263A+Y429F mutant) complexed with YAP(wildtype): The role of residual…x-ray diffractionL—3 (best 0.40)
6GE6X-ray structure of TEAD4(E263A+Y429F mutant) complexed with YAP(WILDTYPE): the role of residual…x-ray diffractionL——
6GECTEAD4 (216-434) complexed with yap peptide (60-100);S94A and myristoate (covalently bound) at 1.70A…x-ray diffractionLACE—
6GEETEAD4 (216-434);E263A complexed with yap peptide (60-100); S94A and myristoate (covalently bound)…x-ray diffractionLACE—
6GEGTEAD4 (216-434);Y429F complexed with yap peptide (60-100); S94A and myristoate (covalently bound)…x-ray diffractionLACE—
6GEITEAD4 (216-434);E263A+Y429F complexed with yap peptide (60- 100);S94A and myristoate (covalently…x-ray diffractionLACE—
6GEKTEAD4 (216-434);Y429F complexed with yap peptide (60-100) and myristoate (covalently bound) at…x-ray diffractionL, M——
6HIKX-ray structure of TEAD4(Y429H) mutant) complexed with YAP (wildtype): Molecular and structural…x-ray diffractionL—1 (best 0.34)
6HIKX-ray structure of TEAD4(Y429H) mutant) complexed with yap (wildtype): molecular and structural…x-ray diffractionLACE—
6HILX-ray structure of TEAD1(Y421H mutant) complexed with YAP(wildtype): Molecular and structural…x-ray diffractionL, O, M, N—5 (best 0.70)
6HILX-ray structure of TEAD1(Y421H mutant) complexed with YAP(WILDTYPE): molecular and structural…x-ray diffractionL, O, M, N——
6Q2XTEAD4 (216-434) complexed with yap peptide (60-100) and myristoate (covalently bound) at 2.1A…x-ray diffractionL——
P46937AlphaFold monomer V2.0 prediction for transcriptional coactivator YAP1 (P46937)———

Ligands

  • ACE · Acetyl group · in 5 records
  • EOE · Beta3-proline · in 2 records

Elsewhere

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