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Crystal structure of tr-alpha bound to T3 in a second site

Analyse Crystal structure of tr-alpha bound to T3 in a second site in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4LNW
Type: protein
Length: 263 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Thyroid hormone receptor alpha
UniProt: P10827
Ligands: T3
Pockets: 3 · best druggability 0.80

Structure

x-ray diffraction · 1 distinct chain · 65% helix, 5% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Thyroid hormone receptor alpha	protein	263	65% helix, 5% strand	P10827

Ligands and binding sites

T3 · 3,5,3'triiodothyronine · ligand · 2 copies · 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	313	0.80	0.90	46	T3
2	131	0.44	0.77	24	empty
3	58	0.33	0.76	13	empty

Modifications

Observed in the structure: 4 modified (artifact).

Compared structures

4LNW · Crystal structure of TR-alpha bound to T3 in a second site · the same entry in another collection · chain A against A, TM-score 1.00
P10827 · AlphaFold monomer V2.0 prediction for thyroid hormone receptor alpha (P10827) · a predicted model of the same protein · chain A against A, TM-score 0.88

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 P10827
Elsewhere: RCSB PDB 4LNW · PDBe 4LNW · UniProt P10827

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