Research workbench
Crystal structure of human ORP1-ORD in complex with cholesterol at 2.6 A resolution
Analyse Crystal structure of human ORP1-ORD in complex with cholesterol at 2.6 A… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5ZM5
- Type
- protein
- Length
- 398 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2.6
- Source
- Homo sapiens
- Molecule
- Oxysterol-binding protein-related protein 1
- UniProt
- Q9BXW6
- Ligands
- CLR
- Pockets
- 4 · best druggability 0.81
Structure
x-ray diffraction · resolution 2.6 · 1 distinct chain · 29% helix, 31% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Oxysterol-binding protein-related protein 1 | protein | 398 | 29% helix, 31% strand | Q9BXW6 |
Ligands and binding sites
- CLR · Cholesterol · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 352 | 0.81 | 0.90 | 41 | CLR |
| 2 | 87 | 0.51 | 0.83 | 31 | empty |
| 3 | 59 | 0.42 | 0.81 | 13 | empty |
| 4 | 77 | 0.40 | 0.78 | 16 | empty |
Modifications
Observed in the structure: 5 modified (artifact).
Compared structures
- 5ZM5 · Crystal structure of human ORP1-ord in complex with cholesterol at 2.6 a resolution · the same entry in another collection · chain A against A, TM-score 1.00
- Q9BXW6 · AlphaFold monomer V2.0 prediction for oxysterol-binding protein- related protein 1… · a predicted model of the same protein · chain A against A, TM-score 0.95
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 Q9BXW6
- Elsewhere: RCSB PDB 5ZM5 · PDBe 5ZM5 · UniProt Q9BXW6
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