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Crystal Structure of Human KEAP1 BTB Domain in Complex with isoxazoline-based inhibitor
Analyse Crystal Structure of Human KEAP1 BTB Domain in Complex with isoxazoline-based… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6FFM
- Type
- protein
- Length
- 131 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2.2
- Source
- Homo sapiens
- Molecule
- Kelch-like ECH-associated protein 1
- UniProt
- Q14145
- Ligands
- D8N
Structure
x-ray diffraction · resolution 2.2 · 1 distinct chain · 52% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Kelch-like ECH-associated protein 1 | protein | 131 | 52% helix, 16% strand | Q14145 |
Ligands and binding sites
- D8N · ~{N}-[4-[(5~{R})-4,5-dihydro-1,2-oxazol-5-yl]phenyl]ethanamide · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Modifications
Observed in the structure: 1 covalent (covalent ligand).
Compared structures
- 6FFM · Crystal structure of human KEAP1 btb domain in complex with isoxazoline-based inhibitor · the same entry in another collection · chain A against A, TM-score 1.00
- Q14145 · AlphaFold monomer V2.0 prediction for kelch-like ech-associated protein 1 (Q14145) · a predicted model of the same protein · chain A against A, TM-score 0.93
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 6FFM · PDBe 6FFM · UniProt Q14145
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