MolNFT v1 · #165159 · protein

ROR(GAMMA)T ligand binding domain in complex with cholesterol and allosteric ligand glenmark

6TLQ · Nuclear receptor ror-gamma: “ROR(GAMMA)T ligand binding domain in complex with cholesterol and allosteric ligand glenmark”. X-ray diffraction, 2 ligands (CLR, MJE), 4 pockets (best druggability 0.82). MolNFT v1 #165159 on GenesisL1…

PDB: 6TLQ
Type: protein
Length: 240 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Nuclear receptor ror-gamma
UniProt: P51449
Ligands: CLR, MJE
Pockets: 4 · best druggability 0.82

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	240	71% helix, 4% strand	P51449

Ligands and binding sites

CLR · Cholesterol · ligand · chains A
MJE · 4-[1-[2,6-bis(chloranyl)phenyl]carbonyl-5-methyl-thieno[3,2-c]pyrazol-3-yl]benzoic acid · ligand · chains A
GOL · Glycerol · additive · 3 copies · 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	385	0.82	0.90	34	CLR, GOL
2	236	0.78	0.91	32	MJE
3	145	0.45	0.76	19	empty
4	60	0.35	0.78	15	GOL

Compared structures

6TLQ · ROR(gamma)t ligand binding domain in complex with cholesterol and allosteric ligand… · 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 6TLQ · PDBe 6TLQ · UniProt P51449

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