MolNFT v1 · #96186 · protein
OSH4 bound to an electrophilic oxysterol
4JCH · Protein KES1: “OSH4 bound to an electrophilic oxysterol”. X-ray diffraction, 1 ligand (1KG), 12 pockets (best druggability 0.84). MolNFT v1 #96186 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 4JCH
- Type
- protein
- Length
- 866 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein KES1
- UniProt
- P35844
- Ligands
- 1KG
- Pockets
- 12 · best druggability 0.84
Structure
x-ray diffraction · 2 distinct chains · 32% helix, 28% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein KES1 | protein | 436 | 31% helix, 28% strand | P35844 |
| B | Protein KES1 | protein | 430 | 33% helix, 28% strand | P35844 |
Ligands and binding sites
- 1KG · (3beta,9beta,22R,25R)-3-hydroxyfurost-5-en-27-yl propanoate · ligand · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
12 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 550 | 0.84 | 0.90 | 56 | 1KG |
| 2 | 596 | 0.83 | 0.88 | 70 | 1KG |
| 3 | 794 | 0.73 | 0.78 | 91 | empty |
| 4 | 572 | 0.72 | 0.80 | 56 | empty |
| 5 | 611 | 0.69 | 0.77 | 52 | empty |
Interfaces
1 interface between chains.
- A–B · 805 Ų buried · 10 hydrogen bonds · protein-protein
Compared structures
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 P35844
- Elsewhere: RCSB PDB 4JCH · PDBe 4JCH · UniProt P35844
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