Research workbench
Crystal structure of the ligand binding domain of polyandrocarpa misakiensis rxr in tetramer in absence of ligand
Analyse Crystal structure of the ligand binding domain of polyandrocarpa misakiensis… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2Q60
- Type
- protein
- Length
- 796 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Retinoid X receptor
- UniProt
- Q9UAF1
- Pockets
- 15 · best druggability 0.79
Structure
x-ray diffraction · 4 distinct chains · 61% helix, 2% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Retinoid X receptor | protein | 198 | 61% helix, 1% strand | Q9UAF1 |
| B | Retinoid X receptor | protein | 198 | 65% helix, 3% strand | Q9UAF1 |
| C | Retinoid X receptor | protein | 203 | 58% helix, 0% strand | Q9UAF1 |
| D | Retinoid X receptor | protein | 197 | 61% helix, 2% strand | Q9UAF1 |
Pockets
15 pockets found on a 1 Å grid, 11 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 685 | 0.79 | 0.83 | 66 | empty |
| 2 | 431 | 0.74 | 0.84 | 47 | empty |
| 3 | 408 | 0.66 | 0.79 | 39 | empty |
| 4 | 211 | 0.65 | 0.83 | 35 | empty |
| 5 | 233 | 0.64 | 0.82 | 27 | empty |
Interfaces
5 interfaces between chains.
- C–D · 1098 Ų buried · 8 hydrogen bonds · protein-protein
- A–B · 1077 Ų buried · 9 hydrogen bonds · protein-protein
- A–C · 873 Ų buried · 3 hydrogen bonds · protein-protein
- B–D · 662 Ų buried · 4 hydrogen bonds · protein-protein
- B–C · 72 Ų buried · 1 hydrogen bond · protein-protein
Compared structures
- 2Q60 · Crystal structure of the ligand binding domain of polyandrocarpa misakiensis rxr in… · 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 Q9UAF1
- Elsewhere: RCSB PDB 2Q60 · PDBe 2Q60 · UniProt Q9UAF1
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