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
- 6S60
- Type
- protein
- Length
- 418 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2
- Source
- Homo sapiens
- Molecule
- Transcriptional enhancer factor TEF-4
- UniProt
- Q15562
- Ligands
- MYR, KX8
- Pockets
- 5 · best druggability 0.83
Structure
x-ray diffraction · resolution 2 · 2 distinct chains · 18% helix, 48% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Transcriptional enhancer factor TEF-4 | protein | 204 | 17% helix, 50% strand | Q15562 |
| B | Transcriptional enhancer factor TEF-4 | protein | 214 | 18% helix, 46% strand | Q15562 |
Ligands and binding sites
- MYR · Myristic acid · ligand · 2 copies · chains A, B
- KX8 · 4-[3-(3,4-dichlorophenyl)-4-[(phenylmethyl) carbamoyl]pyrazol-1-yl]butanoic acid · ligand · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 194 | 0.83 | 0.96 | 36 | MYR |
| 2 | 724 | 0.77 | 0.82 | 75 | MYR |
| 3 | 489 | 0.70 | 0.80 | 50 | empty |
| 4 | 85 | 0.35 | 0.75 | 16 | empty |
| 5 | 77 | 0.35 | 0.75 | 17 | KX8 |
Interfaces
1 interface between chains.
- A–B · 747 Ų buried · 5 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 lipid (myristoylation).
Compared structures
- 6S60 · 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 6S60 · PDBe 6S60 · UniProt Q15562
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.