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ROR(GAMMA)T ligand binding domain in complex with allosteric ligand FM217

Analyse ROR(GAMMA)T ligand binding domain in complex with allosteric ligand FM217 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7NEC
Type: protein
Length: 242 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Nuclear receptor ror-gamma
UniProt: P51449
Ligands: U95
Pockets: 4 · best druggability 0.81

Structure

x-ray diffraction · 1 distinct chain · 71% helix, 4% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Nuclear receptor ror-gamma	protein	242	71% helix, 4% strand	P51449

Ligands and binding sites

U95 · 4-[[3-[2-chloranyl-6-(trifluoromethyl)phenyl]-5-(1~{H}-pyrrol-2-yl)-1,2-oxazol-4-yl]methoxy]benzoic acid · 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, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	361	0.81	0.90	33	empty
2	246	0.78	0.90	33	U95
3	135	0.43	0.75	18	empty
4	63	0.37	0.79	17	empty

Compared structures

7NEC · ROR(gamma)t ligand binding domain in complex with allosteric ligand FM217 · 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 P51449
Elsewhere: RCSB PDB 7NEC · PDBe 7NEC · UniProt P51449

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