Research workbench
Crystal structure of the ligand binding domain of the ultraspiracle protein usp, the ortholog of rxrs in insects
Analyse Crystal structure of the ligand binding domain of the ultraspiracle protein… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1G2N
- Type
- protein
- Length
- 246 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Ultraspiracle protein
- UniProt
- Q7SIF6
- Ligands
- EPH
- Pockets
- 3 · best druggability 0.83
Structure
x-ray diffraction · 1 distinct chain · 64% helix, 4% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Ultraspiracle protein | protein | 246 | 64% helix, 4% strand | Q7SIF6 |
Ligands and binding sites
- EPH · L-alpha-phosphatidyl-beta-oleoyl-gamma-palmitoyl-phosphatidylethanolamine · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 516 | 0.83 | 0.89 | 35 | EPH |
| 2 | 266 | 0.56 | 0.77 | 26 | empty |
| 3 | 124 | 0.42 | 0.76 | 25 | empty |
Compared structures
- 1G2N · Crystal structure of the ligand binding domain of the ultraspiracle protein usp, the… · 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 Q7SIF6
- Elsewhere: RCSB PDB 1G2N · PDBe 1G2N · UniProt Q7SIF6
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