MolNFT v1 · #139107 · protein
Crystal structure of the KEAP1 kelch domain in complex with a tetrapeptide
5X54 · Kelch-like ech-associated protein 1: “Crystal structure of the KEAP1 kelch domain in complex with a tetrapeptide”. X-ray diffraction, 1 ligand (ACE), 3 pockets (best druggability 0.72). MolNFT v1 #139107 on GenesisL1: 3D structure…
- PDB
- 5X54
- Type
- protein
- Length
- 578 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Kelch-like ech-associated protein 1; ACE-glu-TRP-TRP-TRP
- UniProt
- Q14145
- Ligands
- ACE
- Pockets
- 3 · best druggability 0.72
Structure
x-ray diffraction · 2 distinct chains · 1% helix, 51% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Kelch-like ech-associated protein 1 | protein | 285 | 1% helix, 52% strand | Q14145 |
| C, D | ACE-glu-TRP-TRP-TRP | protein | 4 | 0% helix, 0% strand | — |
Ligands and binding sites
- ACE · Acetyl group · ligand · 2 copies · chains C, D
- ACT · Acetate ion · additive · 2 copies · chains B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 394 | 0.72 | 0.83 | 38 | empty |
| 2 | 500 | 0.71 | 0.80 | 50 | empty |
| 3 | 224 | 0.57 | 0.79 | 40 | empty |
Interfaces
3 interfaces between chains.
- A–B · 652 Ų buried · 8 hydrogen bonds · protein-protein
- B–D · 506 Ų buried · 11 hydrogen bonds · protein-protein
- A–C · 486 Ų buried · 12 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 covalent (covalent ligand).
Compared structures
- 5X54 · Crystal structure of the Keap1 Kelch domain in complex with a tetrapeptide · 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 5X54 · PDBe 5X54 · UniProt Q14145
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