Research workbench

ETHR2 in complex with compound 2 (BDM72201)

Analyse ETHR2 in complex with compound 2 (BDM72201) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6HRX
Type: protein
Length: 383 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Probable transcriptional regulatory protein
UniProt: O53623
Ligands: GO8
Pockets: 2 · best druggability 0.85

Structure

x-ray diffraction · 2 distinct chains · 84% helix, 1% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Probable transcriptional regulatory protein	protein	193	84% helix, 0% strand	O53623
B	Probable transcriptional regulatory protein	protein	190	84% helix, 1% strand	O53623

Ligands and binding sites

GO8 · 8-propan-2-ylsulfanyl-7~{H}-purin-6-amine · ligand · 2 copies · chains A, B

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

Pockets

2 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	271	0.85	0.96	51	GO8
2	153	0.81	0.97	27	GO8

Interfaces

1 interface between chains.

A–B · 1425 Å² buried · 7 hydrogen bonds · protein-protein

Compared structures

6HRX · EthR2 in complex with compound 2 (BDM72201) · 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 O53623
Elsewhere: RCSB PDB 6HRX · PDBe 6HRX · UniProt O53623

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