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Crystal structure of qscr bound to agonist S3

Analyse Crystal structure of qscr bound to agonist S3 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6CBQ
Type: protein
Length: 468 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Luxr family transcriptional regulator
UniProt: Q9RMS5
Ligands: EVY
Pockets: 10 · best druggability 0.81

Structure

x-ray diffraction · 1 distinct chain · 57% helix, 14% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Luxr family transcriptional regulator	protein	234	57% helix, 14% strand	Q9RMS5

Ligands and binding sites

EVY · (2S)-2-hexyl-N-[(3S)-2-oxooxolan-3-yl]decanamide · ligand · 2 copies · chains A, B

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

Pockets

10 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	220	0.81	0.94	27	empty
2	181	0.79	0.94	30	EVY
3	174	0.78	0.94	31	EVY
4	253	0.74	0.88	38	empty
5	148	0.41	0.74	29	empty

Interfaces

1 interface between chains.

A–B · 1613 Å² buried · 10 hydrogen bonds · protein-protein

Compared structures

6CBQ · Crystal structure of QscR bound to agonist S3 · 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 Q9RMS5
Elsewhere: RCSB PDB 6CBQ · PDBe 6CBQ · UniProt Q9RMS5

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