Research workbench

Two rth mutants with impaired hormone binding

Analyse Two rth mutants with impaired hormone binding in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1NQ2
Type: protein
Length: 255 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Thyroid hormone receptor beta-1
UniProt: P10828
Ligands: 4HY, ARS, NA
Pockets: 3 · best druggability 0.83

Structure

x-ray diffraction · 1 distinct chain · 64% helix, 4% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Thyroid hormone receptor beta-1	protein	255	64% helix, 4% strand	P10828

Ligands and binding sites

4HY · [4-(4-hydroxy-3-iodo-phenoxy)-3,5-diiodo-phenyl]-acetic acid · ligand · chains A
ARS · Arsenic · metal · 5 copies · 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	191	0.83	0.96	29	4HY
2	96	0.38	0.76	20	empty
3	83	0.36	0.75	16	empty

Compared structures

1NQ2 · Two RTH Mutants with Impaired Hormone Binding · the same entry in another collection · chain A against A, TM-score 1.00
P10828 · AlphaFold monomer V2.0 prediction for thyroid hormone receptor beta (P10828) · a predicted model of the same protein · chain A against A, TM-score 0.95

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 P10828
Elsewhere: RCSB PDB 1NQ2 · PDBe 1NQ2 · UniProt P10828

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.