Research workbench
Kelch domain of human KEAP1 bound to NRF2 linear peptide, ac-gdeetge- NH2
Analyse Kelch domain of human KEAP1 bound to NRF2 linear peptide, ac-gdeetge- NH2 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7K2D
- Type
- protein
- Length
- 570 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Kelch-like ech-associated protein 1; NRF2 linear peptide, ACE-gdeetge-NH2
- UniProt
- Q14145
- Ligands
- ACE, NH2
- Pockets
- 8 · best druggability 0.74
Structure
x-ray diffraction · 3 distinct chains · 0% helix, 52% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Kelch-like ech-associated protein 1 | protein | 283 | 0% helix, 52% strand | Q14145 |
| B | Kelch-like ech-associated protein 1 | protein | 280 | 0% helix, 53% strand | Q14145 |
| P | NRF2 linear peptide, ACE-gdeetge-NH2 | protein | 7 | 0% helix, 0% strand | — |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
8 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 416 | 0.74 | 0.84 | 51 | empty |
| 2 | 369 | 0.72 | 0.84 | 36 | empty |
| 3 | 165 | 0.65 | 0.85 | 23 | empty |
| 4 | 133 | 0.44 | 0.76 | 20 | empty |
| 5 | 129 | 0.41 | 0.75 | 18 | empty |
Interfaces
2 interfaces between chains.
- A–B · 690 Ų buried · 5 hydrogen bonds · protein-protein
- B–P · 472 Ų buried · 15 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 covalent (covalent ligand).
Compared structures
- 7K2D · Kelch domain of human KEAP1 bound to Nrf2 linear peptide, Ac-GDEETGE-NH2 · 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 7K2D · PDBe 7K2D · UniProt Q14145
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