Research workbench
Crystal structure of OSH1 ord domain in complex with cholesterol
Analyse Crystal structure of OSH1 ord domain in complex with cholesterol in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5WVR
- Type
- protein
- Length
- 417 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- KLLA0C04147P
- UniProt
- Q6CUK7
- Ligands
- CLR, SO4
- Pockets
- 6 · best druggability 0.85
Structure
x-ray diffraction · 1 distinct chain · 25% helix, 29% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | KLLA0C04147P | protein | 417 | 25% helix, 29% strand | Q6CUK7 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 338 | 0.85 | 0.94 | 44 | CLR |
| 2 | 204 | 0.54 | 0.78 | 37 | SO4 |
| 3 | 175 | 0.48 | 0.76 | 27 | empty |
| 4 | 118 | 0.45 | 0.78 | 23 | empty |
| 5 | 66 | 0.36 | 0.78 | 19 | empty |
Compared structures
- 5WVR · Crystal structure of Osh1 ORD domain in complex with cholesterol · 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 Q6CUK7
- Elsewhere: RCSB PDB 5WVR · PDBe 5WVR · UniProt Q6CUK7
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