Research workbench
KEAP1 in complex with peptide 8
Analyse KEAP1 in complex with peptide 8 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6T7V
- Type
- protein
- Length
- 294 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Kelch-like ech-associated protein 1; Leu-asp-pro-glu-thr-gly-glu-phe-leu
- UniProt
- Q14145
- Pockets
- 2 · best druggability 0.74
Structure
x-ray diffraction · 2 distinct chains · 0% helix, 51% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Kelch-like ech-associated protein 1 | protein | 285 | 0% helix, 52% strand | Q14145 |
| I | Leu-asp-pro-glu-thr-gly-glu-phe-leu | protein | 9 | 0% helix, 0% strand | — |
Ligands and binding sites
- ACT · Acetate ion · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 447 | 0.74 | 0.83 | 40 | empty |
| 2 | 89 | 0.35 | 0.75 | 22 | empty |
Interfaces
1 interface between chains.
- A–I · 564 Ų buried · 13 hydrogen bonds · protein-protein
Compared structures
- 6T7V · KEAP1 in complex with peptide 8 · 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 6T7V · PDBe 6T7V · UniProt Q14145
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