Research workbench
Kelch domain of human KEAP1 bound to mutant NRF2 eage peptide
Analyse Kelch domain of human KEAP1 bound to mutant NRF2 eage peptide in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5WG1
- Type
- protein
- Length
- 578 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Kelch-like ech-associated protein 1; NRF2 eage mutant peptide
- UniProt
- Q14145
- Ligands
- SO4
- Pockets
- 8 · best druggability 0.76
Structure
x-ray diffraction · 3 distinct chains · 0% helix, 51% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Kelch-like ech-associated protein 1 | protein | 280 | 0% helix, 50% strand | Q14145 |
| B | Kelch-like ech-associated protein 1 | protein | 289 | 0% helix, 53% strand | Q14145 |
| P | NRF2 eage mutant peptide | protein | 9 | 0% helix, 0% strand | — |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
8 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 598 | 0.76 | 0.83 | 61 | empty |
| 2 | 406 | 0.71 | 0.82 | 36 | empty |
| 3 | 269 | 0.69 | 0.84 | 35 | empty |
| 4 | 112 | 0.50 | 0.81 | 29 | empty |
| 5 | 138 | 0.42 | 0.75 | 22 | empty |
Interfaces
2 interfaces between chains.
- A–P · 566 Ų buried · 14 hydrogen bonds · protein-protein
- A–B · 531 Ų buried · 2 hydrogen bonds · protein-protein
Compared structures
- 5WG1 · Kelch domain of human Keap1 bound to mutant Nrf2 EAGE peptide · 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 5WG1 · PDBe 5WG1 · UniProt Q14145
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