Research workbench

Identification of a novel allosteric binding site for rorgt inhibitors

Analyse Identification of a novel allosteric binding site for rorgt inhibitors in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5C4S
Type: protein
Length: 241 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Nuclear receptor ror-gamma
UniProt: P51449
Ligands: 4Y5
Pockets: 5 · best druggability 0.82

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	241	70% helix, 4% strand	P51449

Ligands and binding sites

4Y5 · 4-{1-[2-chloro-6-(trifluoromethyl)benzoyl]-4-fluoro-1H-indazol-3-yl}-3-fluorobenzoic acid · ligand · chains A
GOL · Glycerol · additive · 2 copies · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

5 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	400	0.82	0.90	38	GOL
2	202	0.80	0.93	28	4Y5
3	181	0.54	0.79	20	empty
4	72	0.40	0.79	15	empty
5	87	0.33	0.74	17	empty

Compared structures

5C4S · Identification of a Novel Allosteric Binding Site for RORgt Inhibitors · 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 5C4S · PDBe 5C4S · UniProt P51449

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