Research workbench
KEAP1 in complex with compound 23
Analyse KEAP1 in complex with compound 23 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6SP4
- Type
- protein
- Length
- 1,707 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Kelch-like ech-associated protein 1
- UniProt
- Q14145
- Ligands
- LQK
- Pockets
- 14 · best druggability 0.84
Structure
x-ray diffraction · 3 distinct chains · 0% helix, 50% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C, D, E | Kelch-like ech-associated protein 1 | protein | 284 | 0% helix, 47% strand | Q14145 |
| B | Kelch-like ech-associated protein 1 | protein | 285 | 0% helix, 53% strand | Q14145 |
| F | Kelch-like ech-associated protein 1 | protein | 286 | 0% helix, 49% strand | Q14145 |
Ligands and binding sites
- LQK · (1~{S},2~{R})-2-[[(1~{S})-1-[[1,3-bis(oxidanylidene) isoindol-2-yl]methyl]-5-(2-hydroxyethyloxy)-3,4-dihydro-1~{H}-isoquinolin-2-yl]carbonyl]cyclobutane-1-carboxamide · ligand · 6 copies · chains A, B, C, D, E, F
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
14 pockets found on a 1 Å grid, 10 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1017 | 0.84 | 0.85 | 95 | LQK |
| 2 | 685 | 0.82 | 0.87 | 86 | LQK |
| 3 | 767 | 0.82 | 0.85 | 81 | LQK |
| 4 | 597 | 0.78 | 0.84 | 54 | LQK |
| 5 | 387 | 0.77 | 0.87 | 54 | LQK |
Interfaces
9 interfaces between chains.
- C–D · 442 Ų buried · 6 hydrogen bonds · protein-protein
- A–B · 416 Ų buried · 5 hydrogen bonds · protein-protein
- C–F · 415 Ų buried · 5 hydrogen bonds · protein-protein
- A–D · 404 Ų buried · 2 hydrogen bonds · protein-protein
- E–F · 381 Ų buried · 7 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 3 disulfide (disulfide).
Compared structures
- 6SP4 · KEAP1 in complex with compound 23 · 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 6SP4 · PDBe 6SP4 · UniProt Q14145
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