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X-ray co-structure of nuclear receptor ror-gammat ligand binding domain with a inverse agonist and SRC2 peptide

Analyse X-ray co-structure of nuclear receptor ror-gammat ligand binding domain with a… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5VQK
Type: protein
Length: 256 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Nuclear receptor ror-gamma, SRC2 chimera
UniProt: P51449
Ligands: 9GV
Pockets: 3 · best druggability 0.83

Structure

x-ray diffraction · 1 distinct chain · 71% helix, 4% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Nuclear receptor ror-gamma, SRC2 chimera	protein	256	71% helix, 4% strand	P51449

Ligands and binding sites

9GV · 1-(4-fluorophenyl)-7-methoxy-N-{[4-(methylsulfamoyl) phenyl]methyl}-1H-pyrazolo[3,4-c]pyridine-4-carboxamide · ligand · 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, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	327	0.83	0.92	35	9GV
2	185	0.51	0.77	18	empty
3	66	0.37	0.78	15	empty

Compared structures

5VQK · X-ray co-structure of nuclear receptor ROR-gammat Ligand Binding Domain with a inverse… · 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 5VQK · PDBe 5VQK · UniProt P51449

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