MolNFT v1 · #163695 · protein

ROR(GAMMA)T ligand binding domain in complex with allosteric ligand FM26

6SAL · Nuclear receptor ror-gamma: “ROR(GAMMA)T ligand binding domain in complex with allosteric ligand FM26”. X-ray diffraction, 1 ligand (L3E), 4 pockets (best druggability 0.81). MolNFT v1 #163695 on GenesisL1: 3D structure, binding…

PDB: 6SAL
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: L3E
Pockets: 4 · best druggability 0.81

Structure

x-ray diffraction · 1 distinct chain · 70% helix, 4% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Nuclear receptor ror-gamma	protein	242	70% helix, 4% strand	P51449

Ligands and binding sites

L3E · 4-[(~{E})-[3-[2-chloranyl-6-(trifluoromethyl)phenyl]-5-(1~{H}-pyrrol-3-yl)-1,2-oxazol-4-yl]methylideneamino]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	374	0.81	0.90	34	empty
2	243	0.77	0.90	32	L3E
3	202	0.48	0.75	21	empty
4	51	0.34	0.79	15	empty

Compared structures

6SAL · ROR(gamma)t ligand binding domain in complex with allosteric ligand FM26 · 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 6SAL · PDBe 6SAL · UniProt P51449

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