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Crystal structure of the ROR(GAMMA)T ligand binding domain in complex with 4-(1-(2-chloro-6-(TRIFLUOROMETHYL)BENZOYL)-1H-indazol-3-yl) benzoic acid

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

PDB: 4YPQ
Type: protein
Length: 243 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Nuclear receptor ror-gamma
UniProt: P51449
Ligands: 4F1, MG
Pockets: 4 · best druggability 0.80

Structure

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

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Nuclear receptor ror-gamma	protein	243	69% helix, 4% strand	P51449

Ligands and binding sites

4F1 · 4-{1-[2-chloro-6-(trifluoromethyl)benzoyl]-1H-indazol-3-yl}benzoic acid · ligand · chains A
MG · Magnesium ion · metal · 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	333	0.80	0.89	36	empty
2	242	0.79	0.91	29	4F1
3	89	0.40	0.77	15	empty
4	79	0.34	0.75	13	empty

Compared structures

4YPQ · Crystal structure of the ROR(gamma)t ligand binding domain in complex with… · 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 4YPQ · PDBe 4YPQ · UniProt P51449

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