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Crystal structure of tr-alfa bound to the selective thyromimetic triac

Analyse Crystal structure of tr-alfa bound to the selective thyromimetic triac in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3JZB
Type: protein
Length: 264 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Thra protein
UniProt: Q6FH41
Ligands: 4HY
Pockets: 5 · best druggability 0.83

Structure

x-ray diffraction · 1 distinct chain · 63% helix, 5% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Thra protein	protein	264	63% helix, 5% strand	Q6FH41

Ligands and binding sites

4HY · [4-(4-hydroxy-3-iodo-phenoxy)-3,5-diiodo-phenyl]-acetic acid · ligand · chains A

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

Pockets

5 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	176	0.83	0.97	25	4HY
2	154	0.47	0.77	23	empty
3	107	0.41	0.76	20	empty
4	55	0.38	0.80	13	empty
5	50	0.26	0.74	13	empty

Modifications

Observed in the structure: 4 modified (artifact).

Compared structures

3JZB · Crystal Structure of TR-alfa bound to the selective thyromimetic TRIAC · 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 Q6FH41
Elsewhere: RCSB PDB 3JZB · PDBe 3JZB · UniProt Q6FH41

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