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Crystal structure of TEAD2 bound to compound 2

Analyse Crystal structure of TEAD2 bound to compound 2 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6UYC
Type: protein
Length: 404 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
UniProt: Q15562
Ligands: QLV

Structure

x-ray diffraction · 2 distinct chains.

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	—	protein	211	—	Q15562
B	—	protein	193	—	Q15562

Ligands and binding sites

QLV · N-{5-[(E)-2-(4,4-difluorocyclohexyl)ethenyl]-6-methoxypyridin-3-yl}methanesulfonamide · ligand · 2 copies · chains A, B
TRS · 2-amino-2-hydroxymethyl-propane-1,3-diol · additive · chains B

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Compared structures

6UYC · Crystal structure of TEAD2 bound to Compound 2 · the same entry in another collection · chain A against A, TM-score 1.00
Q15562 · AlphaFold monomer V2.0 prediction for transcriptional enhancer factor tef-4 (Q15562) · a predicted model of the same protein · chain B against A, TM-score 0.98

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt Q15562
Elsewhere: RCSB PDB 6UYC · PDBe 6UYC · UniProt Q15562

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