Research workbench
Kelch domain of human KEAP1 bound to NRF2-based cyclic peptide, C[LHA- deetge]
Analyse Kelch domain of human KEAP1 bound to NRF2-based cyclic peptide, C[LHA- deetge] in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7K2R
- Type
- protein
- Length
- 580 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Kelch-like ech-associated protein 1; B3A-asp-pro-glu-thr-gly-glu
- UniProt
- Q14145
- Ligands
- SO4
- Pockets
- 5 · best druggability 0.77
Structure
x-ray diffraction · 3 distinct chains · 0% helix, 49% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| B | Kelch-like ech-associated protein 1 | protein | 289 | 0% helix, 49% strand | Q14145 |
| A | Kelch-like ech-associated protein 1 | protein | 284 | 0% helix, 50% strand | Q14145 |
| P | B3A-asp-pro-glu-thr-gly-glu | protein | 7 | 0% helix, 0% strand | — |
Ligands and binding sites
- SO4 · Sulfate ion · ion · chains A, P
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 638 | 0.77 | 0.83 | 76 | empty |
| 2 | 449 | 0.72 | 0.82 | 39 | empty |
| 3 | 126 | 0.53 | 0.81 | 30 | empty |
| 4 | 114 | 0.41 | 0.76 | 23 | empty |
| 5 | 67 | 0.30 | 0.74 | 17 | empty |
Interfaces
2 interfaces between chains.
- B–A · 533 Ų buried · 4 hydrogen bonds · protein-protein
- A–P · 454 Ų buried · 13 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 modified (nonstandard).
Compared structures
- 7K2R · Kelch domain of human KEAP1 bound to Nrf2-based cyclic peptide, c[LhA-DEETGE] · the same entry in another collection · chain B against B, 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 7K2R · PDBe 7K2R · UniProt Q14145
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