Research workbench
Crystal structure of HTEAD2 in complex with a trisubstituted pyrazole inhibitor
Analyse Crystal structure of HTEAD2 in complex with a trisubstituted pyrazole inhibitor in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6S66
- Type
- protein
- Length
- 400 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Transcriptional enhancer factor tef-4
- UniProt
- Q15562
- Ligands
- MYR, KWW
- Pockets
- 6 · best druggability 0.83
Structure
x-ray diffraction · 2 distinct chains · 19% helix, 51% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Transcriptional enhancer factor tef-4 | protein | 192 | 18% helix, 53% strand | Q15562 |
| B | Transcriptional enhancer factor tef-4 | protein | 208 | 19% helix, 49% strand | Q15562 |
Ligands and binding sites
- MYR · Myristic acid · ligand · 2 copies · chains A, B
- KWW · 1-(2-azanylethyl)-3-(3,4-dichlorophenyl)-~{N}-(phenylmethyl)pyrazole-4-carboxamide · ligand · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 184 | 0.83 | 0.97 | 36 | MYR |
| 2 | 212 | 0.82 | 0.95 | 36 | MYR |
| 3 | 348 | 0.66 | 0.81 | 40 | empty |
| 4 | 470 | 0.60 | 0.75 | 52 | empty |
| 5 | 100 | 0.39 | 0.76 | 15 | empty |
Interfaces
1 interface between chains.
- A–B · 771 Ų buried · 8 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 lipid (myristoylation).
Compared structures
- 6S66 · Crystal structure of hTEAD2 in complex with a trisubstituted pyrazole inhibitor · 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 A 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 6S66 · PDBe 6S66 · UniProt Q15562
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