Research workbench
Crystal structure of the KEAP1 complex with a peptide base on etge motif.
Analyse Crystal structure of the KEAP1 complex with a peptide base on etge motif. in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7ECA
- Type
- protein
- Length
- 300 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Kelch-like ech-associated protein 1; Leu-asp-glu-glu-thr-gly-glu-phe-leu-pro
- UniProt
- Q9Z2X8, Q60795
- Ligands
- SO4
- Pockets
- 1 · best druggability 0.74
Structure
x-ray diffraction · 2 distinct chains · 1% helix, 50% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Kelch-like ech-associated protein 1 | protein | 290 | 1% helix, 52% strand | Q9Z2X8 |
| B | Leu-asp-glu-glu-thr-gly-glu-phe-leu-pro | protein | 10 | 0% helix, 0% strand | Q60795 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 11 copies · chains A, B
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 | 507 | 0.74 | 0.83 | 62 | SO4 |
Interfaces
1 interface between chains.
- A–B · 543 Ų buried · 15 hydrogen bonds · protein-protein
Compared structures
- 7ECA · Crystal structure of the Keap1 complex with a peptide base on ETGE motif. · the same entry in another collection · chain A against A, TM-score 1.00
- Q9Z2X8 · AlphaFold monomer V2.0 prediction for kelch-like ech-associated protein 1 (Q9Z2X8) · a predicted model of the same protein · chain A against A, TM-score 1.00
- Q60795 · AlphaFold monomer V2.0 prediction for nuclear factor erythroid 2-related factor 2 (Q60795) · a predicted model of the same protein · chain B against A, TM-score 0.73
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 Q9Z2X8
- Every structure of UniProt Q60795
- Elsewhere: RCSB PDB 7ECA · PDBe 7ECA · UniProt Q9Z2X8 · UniProt Q60795
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