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Structure of tr-alfa bound to selective thyromimetic gc-1 in P212121 space group

Analyse Structure of tr-alfa bound to selective thyromimetic gc-1 in P212121 space group in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3ILZ
Type: protein
Length: 267 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Thyroid hormone receptor, alpha isoform 1 variant
UniProt: Q59FW3
Ligands: B72
Pockets: 5 · best druggability 0.82

Structure

x-ray diffraction · 1 distinct chain · 60% helix, 4% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Thyroid hormone receptor, alpha isoform 1 variant	protein	267	60% helix, 4% strand	Q59FW3

Ligands and binding sites

B72 · {4-[4-hydroxy-3-(1-methylethyl)benzyl]-3,5-dimethylphenoxy}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, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	180	0.82	0.97	32	B72
2	160	0.50	0.78	24	empty
3	89	0.39	0.77	18	empty
4	58	0.36	0.78	14	empty
5	68	0.31	0.75	17	empty

Modifications

Observed in the structure: 4 modified (artifact).

Compared structures

3ILZ · Structure of TR-alfa bound to selective thyromimetic GC-1 in P212121 space group · 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 Q59FW3
Elsewhere: RCSB PDB 3ILZ · PDBe 3ILZ · UniProt Q59FW3

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