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Keap1 - inhibitor complex
Analyse Keap1 - inhibitor complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6HWS
- Type
- protein
- Length
- 285 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.75
- Source
- Homo sapiens
- Molecule
- Kelch-like ECH-associated protein 1
- UniProt
- Q14145
- Ligands
- GX8, NA
- Pockets
- 1 · best druggability 0.73
Structure
x-ray diffraction · resolution 1.75 · 1 distinct chain · 0% helix, 50% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Kelch-like ECH-associated protein 1 | protein | 285 | 0% helix, 50% strand | Q14145 |
Ligands and binding sites
- GX8 · 2-[[4-[2-hydroxy-2-oxoethyl-(4-methoxyphenyl)sulfonyl-amino]-3-phenylmethoxy-phenyl]-(4-methoxyphenyl) sulfonyl-amino]ethanoic acid · ligand · chains A
- NA · Sodium ion · metal · 7 copies · chains A
- EDO · 1,2-ethanediol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 638 | 0.73 | 0.80 | 53 | GX8 |
Compared structures
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 6HWS · PDBe 6HWS · UniProt Q14145
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