MolNFT v1 · #18480 · protein
Human lxr beta hormone receptor complexed with T0901317
1PQC · Oxysterols receptor lxr-beta: “Human lxr beta hormone receptor complexed with T0901317”. X-ray diffraction, 1 ligand (444), 16 pockets (best druggability 0.85). MolNFT v1 #18480 on GenesisL1: 3D structure, binding sites and pockets…
- PDB
- 1PQC
- Type
- protein
- Length
- 920 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Oxysterols receptor lxr-beta
- UniProt
- P55055
- Ligands
- 444
- Pockets
- 16 · best druggability 0.85
Structure
x-ray diffraction · 4 distinct chains · 71% helix, 4% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Oxysterols receptor lxr-beta | protein | 232 | 70% helix, 5% strand | P55055 |
| B | Oxysterols receptor lxr-beta | protein | 238 | 69% helix, 4% strand | P55055 |
| C | Oxysterols receptor lxr-beta | protein | 231 | 69% helix, 4% strand | P55055 |
| D | Oxysterols receptor lxr-beta | protein | 219 | 74% helix, 2% strand | P55055 |
Ligands and binding sites
- 444 · N-(2,2,2-trifluoroethyl)-N-{4-[2,2,2-trifluoro-1-hydroxy-1-(trifluoromethyl) ethyl]phenyl}benzenesulfonamide · ligand · 4 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
16 pockets found on a 1 Å grid, 10 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 222 | 0.85 | 0.97 | 25 | 444 |
| 2 | 225 | 0.84 | 0.96 | 25 | 444 |
| 3 | 314 | 0.84 | 0.94 | 43 | 444 |
| 4 | 376 | 0.84 | 0.92 | 37 | 444 |
| 5 | 1162 | 0.79 | 0.81 | 109 | empty |
Interfaces
3 interfaces between chains.
- C–D · 1100 Ų buried · 7 hydrogen bonds · protein-protein
- A–B · 1071 Ų buried · 6 hydrogen bonds · protein-protein
- B–C · 150 Ų buried · 1 hydrogen bond · 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 P55055
- Elsewhere: RCSB PDB 1PQC · PDBe 1PQC · UniProt P55055
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