Research workbench
Btb domain of KEAP1 in complex with cddo
Analyse Btb domain of KEAP1 in complex with cddo in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4CXT
- Type
- protein
- Length
- 132 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Kelch-like ech-associated protein 1
- UniProt
- Q14145
- Ligands
- SXJ
Structure
x-ray diffraction · 1 distinct chain · 51% helix, 11% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Kelch-like ech-associated protein 1 | protein | 132 | 51% helix, 11% strand | Q14145 |
Ligands and binding sites
- SXJ · (13alpha,18alpha)-2-cyano-3-hydroxy-12-oxooleana-2,9(11)-dien-28-oic acid · 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
- 4CXT · BTB domain of KEAP1 in complex with CDDO · 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 4CXT · PDBe 4CXT · UniProt Q14145
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