Research workbench
Human TEAD3 in complex with 1-cyclopentyl-1H-PYRAZOLO[3,4-B]PYRIDINE- 5-carboxylic acid
Analyse Human TEAD3 in complex with 1-cyclopentyl-1H-PYRAZOLO[3,4-B]PYRIDINE… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7ZJQ
- Type
- protein
- Length
- 835 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Transcriptional enhancer factor tef-5
- UniProt
- Q99594
- Ligands
- JIK
- Pockets
- 10 · best druggability 0.82
Structure
x-ray diffraction · 3 distinct chains · 16% helix, 52% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Transcriptional enhancer factor tef-5 | protein | 210 | 15% helix, 51% strand | Q99594 |
| B | Transcriptional enhancer factor tef-5 | protein | 209 | 17% helix, 52% strand | Q99594 |
| C, D | Transcriptional enhancer factor tef-5 | protein | 208 | 17% helix, 53% strand | Q99594 |
Ligands and binding sites
- JIK · 1-cyclopentylpyrazolo[3,4-b]pyridine-5-carboxylic acid · ligand · 4 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
10 pockets found on a 1 Å grid, 8 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 171 | 0.82 | 0.97 | 35 | JIK |
| 2 | 140 | 0.82 | 0.98 | 29 | JIK |
| 3 | 147 | 0.81 | 0.97 | 27 | JIK |
| 4 | 448 | 0.81 | 0.89 | 68 | JIK |
| 5 | 542 | 0.77 | 0.84 | 58 | empty |
Interfaces
5 interfaces between chains.
- A–B · 800 Ų buried · 20 hydrogen bonds · protein-protein
- A–D · 778 Ų buried · 7 hydrogen bonds · protein-protein
- B–C · 769 Ų buried · 9 hydrogen bonds · protein-protein
- A–C · 206 Ų buried · 5 hydrogen bonds · protein-protein
- B–D · 137 Ų buried · 3 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 modified (oxidation).
Compared structures
- 7ZJQ · Human TEAD3 in complex with 1-Cyclopentyl-1H-pyrazolo[3,4-b]pyridine-5-carboxylic acid · the same entry in another collection · chain A against A, TM-score 1.00
- Q99594 · AlphaFold monomer V2.0 prediction for transcriptional enhancer factor tef-5 (Q99594) · a predicted model of the same protein · chain C against A, TM-score 0.99
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 Q99594
- Elsewhere: RCSB PDB 7ZJQ · PDBe 7ZJQ · UniProt Q99594
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.