Research workbench
Structure of OSH4 with a cholesterol analog
Analyse Structure of OSH4 with a cholesterol analog in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4F4B
- Type
- protein
- Length
- 847 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein KES1
- UniProt
- P35844
- Ligands
- L39
- Pockets
- 11 · best druggability 0.84
Structure
x-ray diffraction · 2 distinct chains · 32% helix, 29% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein KES1 | protein | 422 | 31% helix, 29% strand | P35844 |
| B | Protein KES1 | protein | 425 | 32% helix, 28% strand | P35844 |
Ligands and binding sites
- L39 · (3beta,9beta,25R)-3-hydroxy-26-iodocholest-5-ene-16,22-dione · ligand · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
11 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 673 | 0.84 | 0.88 | 74 | L39 |
| 2 | 747 | 0.83 | 0.86 | 79 | L39 |
| 3 | 596 | 0.74 | 0.81 | 52 | empty |
| 4 | 575 | 0.72 | 0.80 | 53 | empty |
| 5 | 607 | 0.69 | 0.78 | 74 | empty |
Interfaces
1 interface between chains.
- A–B · 856 Ų buried · 9 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 4F4B · PDBe 4F4B · UniProt P35844
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