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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).

ChainMoleculeTypeResiduesSecondary structureUniProt
AUltraspiracle proteinprotein24664% helix, 4% strandQ7SIF6

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.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
15160.830.8935EPH
22660.560.7726empty
31240.420.7625empty

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

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