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Ligand complex of rorg lbd

Analyse Ligand complex of rorg lbd in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6ESN
Type: protein
Length: 264 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Nuclear receptor ror-gamma; Lys-his-lys-ile-leu-his-arg-leu-leu-gln-asp-ser
UniProt: P51449
Ligands: BWE, NA
Pockets: 3 · best druggability 0.82

Structure

x-ray diffraction · 2 distinct chains · 72% helix, 4% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Nuclear receptor ror-gamma	protein	252	73% helix, 4% strand	P51449
C	Lys-his-lys-ile-leu-his-arg-leu-leu-gln-asp-ser	protein	12	58% helix, 0% strand	—

Ligands and binding sites

BWE · (2~{R})-2-acetamido-~{N}-[4-(5-cyano-3-fluoranyl-2-methoxy-phenyl)thiophen-2-yl]-2-(4-ethylsulfonylphenyl)ethanamide · ligand · chains A
NA · Sodium ion · metal · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	367	0.82	0.90	38	BWE
2	163	0.48	0.77	29	empty
3	61	0.37	0.79	15	empty

Interfaces

1 interface between chains.

A–C · 566 Å² buried · 10 hydrogen bonds · protein-protein

Compared structures

6ESN · Ligand complex of RORg LBD · 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 6ESN · PDBe 6ESN · UniProt P51449

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