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Structure of rorgt bound to

Analyse Structure of rorgt bound to in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5UFO
Type
protein
Length
225 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Nuclear receptor ror-gamma
UniProt
P51449
Ligands
87J
Pockets
4 · best druggability 0.83

Structure

x-ray diffraction · 1 distinct chain · 69% helix, 4% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ANuclear receptor ror-gammaprotein22569% helix, 4% strandP51449

Ligands and binding sites

  • 87J · (S)-{4-chloro-2-methoxy-3-[4-(methylsulfonyl)phenyl]quinolin-6-yl}(1-methyl-1H-imidazol-5-yl)[6-(trifluoromethyl)pyridin-3-yl]methanol · 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, 1 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
14040.830.903687J
2960.470.8019empty
3920.420.7919empty
4660.350.7718empty

Compared structures

  • 5UFO · Structure of RORgt bound to · the same entry in another collection · chain A against A, TM-score 1.00

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