Research workbench
Crystal structure of cpd 15 bound to KEAP1 kelch domain
Analyse Crystal structure of cpd 15 bound to KEAP1 kelch domain in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4IN4
- Type
- protein
- Length
- 861 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Kelch-like ech-associated protein 1
- UniProt
- Q14145
- Ligands
- 4ID, PO4
- Pockets
- 6 · best druggability 0.78
Structure
x-ray diffraction · 3 distinct chains · 0% helix, 51% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Kelch-like ech-associated protein 1 | protein | 288 | 1% helix, 49% strand | Q14145 |
| B | Kelch-like ech-associated protein 1 | protein | 284 | 0% helix, 51% strand | Q14145 |
| C | Kelch-like ech-associated protein 1 | protein | 289 | 0% helix, 52% strand | Q14145 |
Ligands and binding sites
- 4ID · 2-({5-[(2,4-dimethylphenyl)sulfonyl]-6-oxo-1,6-dihydropyrimidin-2-yl}sulfanyl)-N-[2-(trifluoromethyl)phenyl]acetamide · ligand · 6 copies · chains A, B, C
- PO4 · Phosphate ion · ion · 8 copies · chains A, B, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 425 | 0.78 | 0.87 | 61 | PO4, 4ID |
| 2 | 351 | 0.77 | 0.88 | 50 | 4ID |
| 3 | 670 | 0.73 | 0.80 | 57 | 4ID |
| 4 | 536 | 0.73 | 0.82 | 64 | PO4 |
| 5 | 152 | 0.55 | 0.81 | 24 | empty |
Interfaces
3 interfaces between chains.
- A–C · 652 Ų buried · 11 hydrogen bonds · protein-protein
- A–B · 652 Ų buried · 6 hydrogen bonds · protein-protein
- B–C · 52 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- 4IN4 · Crystal structure of cpd 15 bound to Keap1 Kelch domain · the same entry in another collection · chain A against A, TM-score 1.00
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 Q14145
- Elsewhere: RCSB PDB 4IN4 · PDBe 4IN4 · UniProt Q14145
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.